Investigating the Transepithelial Transport and Enzymatic Stability of Lactononadecapeptide (NIPPLTQTPVVVPPFLQPE), a 19-Amino Acid Casein-Derived Peptide in Caco‑2 Cells
Lactononadecapeptide (LNDP; NIPPLTQTPVVVPPFLQPE), a casein-derived peptide comprising 19 residues, is known for its capacity to enhance cognitive function. This study aimed to explore the transepithelial transport and stability of LNDP. Results showed that LNDP retained over 90% stability afte...
Saved in:
| Published in | Journal of Agricultural and Food Chemistry Vol. 72; no. 22; pp. 12719 - 12724 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
American Chemical Society
05.06.2024
American Chemical Society (ACS) |
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | Lactononadecapeptide (LNDP; NIPPLTQTPVVVPPFLQPE), a casein-derived peptide comprising 19 residues, is known for its capacity to enhance cognitive function. This study aimed to explore the transepithelial transport and stability of LNDP. Results showed that LNDP retained over 90% stability after 2 h of treatment with gastrointestinal enzymes. The stability of LNDP on Caco-2 cell monolayers ranged from 93.4% ± 0.9% to 101.1% ± 1.2% over a period of 15–60 min, with no significant differences at each time point. The permeability of LNDP across an artificial lipid membrane was very low with the effective permeability of 3.6 × 10–11 cm/s. The Caco-2 assay demonstrated that LNDP could traverse the intestinal epithelium, with an apparent permeability of 1.22 × 10–6 cm/s. Its transport was significantly inhibited to 67.9% ± 5.0% of the control by Gly-Pro, a competitor of peptide transporter 1 (PEPT1). Furthermore, PEPT1 knockdown using siRNA significantly inhibited LNDP transport by 77.6% ± 1.9% in Caco-2 cell monolayers. The LNDP uptake in PEPT1-expressing HEK293 cells was significantly higher (54.5% ± 14.6%) than that in mock cells. These findings suggest that PEPT1 plays a crucial role in LNDP transport, and LNDP exhibits good resistance to gastrointestinal enzymes. |
|---|---|
| AbstractList | Lactononadecapeptide (LNDP; NIPPLTQTPVVVPPFLQPE), a casein-derived peptide comprising 19 residues, is known for its capacity to enhance cognitive function. This study aimed to explore the transepithelial transport and stability of LNDP. Results showed that LNDP retained over 90% stability after 2 h of treatment with gastrointestinal enzymes. The stability of LNDP on Caco-2 cell monolayers ranged from 93.4% ± 0.9% to 101.1% ± 1.2% over a period of 15–60 min, with no significant differences at each time point. The permeability of LNDP across an artificial lipid membrane was very low with the effective permeability of 3.6 × 10–¹¹ cm/s. The Caco-2 assay demonstrated that LNDP could traverse the intestinal epithelium, with an apparent permeability of 1.22 × 10–⁶ cm/s. Its transport was significantly inhibited to 67.9% ± 5.0% of the control by Gly-Pro, a competitor of peptide transporter 1 (PEPT1). Furthermore, PEPT1 knockdown using siRNA significantly inhibited LNDP transport by 77.6% ± 1.9% in Caco-2 cell monolayers. The LNDP uptake in PEPT1-expressing HEK293 cells was significantly higher (54.5% ± 14.6%) than that in mock cells. These findings suggest that PEPT1 plays a crucial role in LNDP transport, and LNDP exhibits good resistance to gastrointestinal enzymes. Lactononadecapeptide (LNDP; NIPPLTQTPVVVPPFLQPE), a casein-derived peptide comprising 19 residues, is known for its capacity to enhance cognitive function. This study aimed to explore the transepithelial transport and stability of LNDP. Results showed that LNDP retained over 90% stability after 2 h of treatment with gastrointestinal enzymes. The stability of LNDP on Caco-2 cell monolayers ranged from 93.4% ± 0.9% to 101.1% ± 1.2% over a period of 15–60 min, with no significant differences at each time point. The permeability of LNDP across an artificial lipid membrane was very low with the effective permeability of 3.6 × 10 –11 cm/s. The Caco-2 assay demonstrated that LNDP could traverse the intestinal epithelium, with an apparent permeability of 1.22 × 10 –6 cm/s. Its transport was significantly inhibited to 67.9% ± 5.0% of the control by Gly-Pro, a competitor of peptide transporter 1 (PEPT1). Furthermore, PEPT1 knockdown using siRNA significantly inhibited LNDP transport by 77.6% ± 1.9% in Caco-2 cell monolayers. The LNDP uptake in PEPT1-expressing HEK293 cells was significantly higher (54.5% ± 14.6%) than that in mock cells. These findings suggest that PEPT1 plays a crucial role in LNDP transport, and LNDP exhibits good resistance to gastrointestinal enzymes. Lactononadecapeptide (LNDP; NIPPLTQTPVVVPPFLQPE), a casein-derived peptide comprising 19 residues, is known for its capacity to enhance cognitive function. This study aimed to explore the transepithelial transport and stability of LNDP. Results showed that LNDP retained over 90% stability after 2 h of treatment with gastrointestinal enzymes. The stability of LNDP on Caco-2 cell monolayers ranged from 93.4% ± 0.9% to 101.1% ± 1.2% over a period of 15-60 min, with no significant differences at each time point. The permeability of LNDP across an artificial lipid membrane was very low with the effective permeability of 3.6 × 10-11 cm/s. The Caco-2 assay demonstrated that LNDP could traverse the intestinal epithelium, with an apparent permeability of 1.22 × 10-6 cm/s. Its transport was significantly inhibited to 67.9% ± 5.0% of the control by Gly-Pro, a competitor of peptide transporter 1 (PEPT1). Furthermore, PEPT1 knockdown using siRNA significantly inhibited LNDP transport by 77.6% ± 1.9% in Caco-2 cell monolayers. The LNDP uptake in PEPT1-expressing HEK293 cells was significantly higher (54.5% ± 14.6%) than that in mock cells. These findings suggest that PEPT1 plays a crucial role in LNDP transport, and LNDP exhibits good resistance to gastrointestinal enzymes.Lactononadecapeptide (LNDP; NIPPLTQTPVVVPPFLQPE), a casein-derived peptide comprising 19 residues, is known for its capacity to enhance cognitive function. This study aimed to explore the transepithelial transport and stability of LNDP. Results showed that LNDP retained over 90% stability after 2 h of treatment with gastrointestinal enzymes. The stability of LNDP on Caco-2 cell monolayers ranged from 93.4% ± 0.9% to 101.1% ± 1.2% over a period of 15-60 min, with no significant differences at each time point. The permeability of LNDP across an artificial lipid membrane was very low with the effective permeability of 3.6 × 10-11 cm/s. The Caco-2 assay demonstrated that LNDP could traverse the intestinal epithelium, with an apparent permeability of 1.22 × 10-6 cm/s. Its transport was significantly inhibited to 67.9% ± 5.0% of the control by Gly-Pro, a competitor of peptide transporter 1 (PEPT1). Furthermore, PEPT1 knockdown using siRNA significantly inhibited LNDP transport by 77.6% ± 1.9% in Caco-2 cell monolayers. The LNDP uptake in PEPT1-expressing HEK293 cells was significantly higher (54.5% ± 14.6%) than that in mock cells. These findings suggest that PEPT1 plays a crucial role in LNDP transport, and LNDP exhibits good resistance to gastrointestinal enzymes. Lactononadecapeptide (LNDP; NIPPLTQTPVVVPPFLQPE), a casein-derived peptide comprising 19 residues, is known for its capacity to enhance cognitive function. This study aimed to explore the transepithelial transport and stability of LNDP. Results showed that LNDP retained over 90% stability after 2 h of treatment with gastrointestinal enzymes. The stability of LNDP on Caco-2 cell monolayers ranged from 93.4% ± 0.9% to 101.1% ± 1.2% over a period of 15-60 min, with no significant differences at each time point. The permeability of LNDP across an artificial lipid membrane was very low with the effective permeability of 3.6 × 10 cm/s. The Caco-2 assay demonstrated that LNDP could traverse the intestinal epithelium, with an apparent permeability of 1.22 × 10 cm/s. Its transport was significantly inhibited to 67.9% ± 5.0% of the control by Gly-Pro, a competitor of peptide transporter 1 (PEPT1). Furthermore, PEPT1 knockdown using siRNA significantly inhibited LNDP transport by 77.6% ± 1.9% in Caco-2 cell monolayers. The LNDP uptake in PEPT1-expressing HEK293 cells was significantly higher (54.5% ± 14.6%) than that in mock cells. These findings suggest that PEPT1 plays a crucial role in LNDP transport, and LNDP exhibits good resistance to gastrointestinal enzymes. Lactononadecapeptide (LNDP; NIPPLTQTPVVVPPFLQPE), a casein-derived peptide comprising 19 residues, is known for its capacity to enhance cognitive function. This study aimed to explore the transepithelial transport and stability of LNDP. Results showed that LNDP retained over 90% stability after 2 h of treatment with gastrointestinal enzymes. The stability of LNDP on Caco-2 cell monolayers ranged from 93.4% ± 0.9% to 101.1% ± 1.2% over a period of 15–60 min, with no significant differences at each time point. The permeability of LNDP across an artificial lipid membrane was very low with the effective permeability of 3.6 × 10–11 cm/s. The Caco-2 assay demonstrated that LNDP could traverse the intestinal epithelium, with an apparent permeability of 1.22 × 10–6 cm/s. Its transport was significantly inhibited to 67.9% ± 5.0% of the control by Gly-Pro, a competitor of peptide transporter 1 (PEPT1). Furthermore, PEPT1 knockdown using siRNA significantly inhibited LNDP transport by 77.6% ± 1.9% in Caco-2 cell monolayers. The LNDP uptake in PEPT1-expressing HEK293 cells was significantly higher (54.5% ± 14.6%) than that in mock cells. These findings suggest that PEPT1 plays a crucial role in LNDP transport, and LNDP exhibits good resistance to gastrointestinal enzymes. |
| Author | Sasai, Masaki Okura, Takashi Hirota, Tatsuhiko Nakatani, Eriko Tanaka, Shimako Miyazaki, Hidetoshi |
| AuthorAffiliation | Asahi Quality and Innovations, Ltd Laboratory of Pharmaceutics, Faculty of Pharmaceutical Sciences Core Technology Laboratories |
| AuthorAffiliation_xml | – name: Laboratory of Pharmaceutics, Faculty of Pharmaceutical Sciences – name: Core Technology Laboratories – name: Asahi Quality and Innovations, Ltd |
| Author_xml | – sequence: 1 givenname: Eriko surname: Nakatani fullname: Nakatani, Eriko email: erikon@pharm.teikyo-u.ac.jp organization: Laboratory of Pharmaceutics, Faculty of Pharmaceutical Sciences – sequence: 2 givenname: Masaki orcidid: 0009-0001-8095-5450 surname: Sasai fullname: Sasai, Masaki organization: Asahi Quality and Innovations, Ltd – sequence: 3 givenname: Hidetoshi surname: Miyazaki fullname: Miyazaki, Hidetoshi organization: Asahi Quality and Innovations, Ltd – sequence: 4 givenname: Shimako surname: Tanaka fullname: Tanaka, Shimako organization: Laboratory of Pharmaceutics, Faculty of Pharmaceutical Sciences – sequence: 5 givenname: Tatsuhiko surname: Hirota fullname: Hirota, Tatsuhiko organization: Asahi Quality and Innovations, Ltd – sequence: 6 givenname: Takashi surname: Okura fullname: Okura, Takashi organization: Laboratory of Pharmaceutics, Faculty of Pharmaceutical Sciences |
| BackLink | https://cir.nii.ac.jp/crid/1873399491341085952$$DView record in CiNii https://www.ncbi.nlm.nih.gov/pubmed/38789103$$D View this record in MEDLINE/PubMed |
| BookMark | eNqFUsFuEzEQtVARTQt3TsgHDkXqBnu96_WeqiikECmCVIRcLa_tTV1t7GXtRAonfoEPyZl7PoUvwSGhAiTgYs9o3nue8bwzcGKd1QA8xaiPUYpfCun7d6KW_UwiVBbZA9DDeYqSHGN2AnooYhKWU3wKzry_QwixvECPwClhBSsxIj3wdWzX2gezEMHYBQy3Gs46Yb1uTYwbI5pD3rouQGEVHNlPm2UES_g-iMo0Jmygq-FEyOBid0JpKVrdBqM0vHg7nu6208lst72ZxWg-n8d0er3bTm5iMHpxCQXEZTJYGuvgQBoFh8JrY5NXujNrreD0qGRsrEj37fOXFA510_jH4GEtGq-fHO9z8OF6NBu-SSbvXo-Hg0kiKKIhyUkqZVrVVYVUTqs4tURpqVRRlZJSwtJKU411JaTKmMqyHCnMKpGnuC4zShk5B1cH3XZVLbWS2oZONLztzFJ0G-6E4b9XrLnlC7fmGOO8iM9HhYujQuc-ruJf86XxMs4grHYrzwnOCcWxlez_UEQRKQhmKEKf_drXfUM_NxsB6ACQnfO-0_U9BCO-Nw-P5uF78_CjeSKF_kGRJsRVu_1kpvkX8fmBaI2JnP2JWUFIWWYlJhmOtivz_U9cHmA_BNyqs3Fzf1f9DutB6wg |
| CitedBy_id | crossref_primary_10_1016_j_lwt_2024_117081 crossref_primary_10_1016_j_foodchem_2025_142935 crossref_primary_10_1016_j_foodres_2025_116065 |
| Cites_doi | 10.1017/S0954422416000032 10.1021/acs.jcim.1c00380 10.1002/jps.20075 10.1016/0006-291X(91)91647-U 10.3390/molecules24152843 10.1002/psc.870 10.1016/j.bbrc.2018.06.118 10.1016/j.coph.2013.08.004 10.1021/pr0705035 10.1002/mnfr.200700503 10.1021/jf703640p 10.1093/bbb/zbaa117 10.1038/368563a0 10.1016/j.ajps.2018.05.008 10.1021/acs.jafc.7b02176 10.1021/acs.jafc.3c04940 10.3390/molecules28031151 10.1016/0016-5085(89)90897-4 10.1007/s11095-005-6156-9 10.1016/0005-2744(74)90053-9 10.1152/ajpgi.00136.2002 10.1074/jbc.273.7.3861 10.1179/1476830514Y.0000000122 10.1016/j.peptides.2022.170843 10.1016/j.foodchem.2015.05.121 10.1083/jcb.102.6.2125 10.1002/psc.371 10.1074/jbc.270.47.28425 10.1271/bbb.66.378 10.1039/b301507f 10.1080/09637486.2017.1324564 10.3168/jds.S0022-0302(96)76585-2 10.1021/acs.jafc.1c08191 10.1002/mnfr.200900443 10.3168/jds.S0022-0302(95)76745-5 10.1021/jf405639w 10.3390/pharmaceutics15102517 10.3168/jds.S0022-0302(04)73453-0 10.1080/09637486.2017.1365824 10.1002/(SICI)1521-3803(19990601)43:3<154::AID-FOOD154>3.0.CO;2-A 10.1002/0471140864.ps2103s25 10.1096/fj.201900621R 10.1016/j.jff.2017.06.001 10.1042/bj2840595 10.1016/j.neurobiolaging.2018.07.016 10.1021/acs.jafc.5b01824 |
| ContentType | Journal Article |
| Copyright | 2024 The Authors. Published by American Chemical Society 2024 The Authors. Published by American Chemical Society 2024 The Authors |
| Copyright_xml | – notice: 2024 The Authors. Published by American Chemical Society – notice: 2024 The Authors. Published by American Chemical Society 2024 The Authors |
| DBID | RYH AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 7S9 L.6 5PM |
| DOI | 10.1021/acs.jafc.4c00974 |
| DatabaseName | CiNii Complete CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic AGRICOLA AGRICOLA - Academic PubMed Central (Full Participant titles) |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
| DatabaseTitleList | AGRICOLA MEDLINE - Academic MEDLINE |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Agriculture |
| EISSN | 1520-5118 |
| EndPage | 12724 |
| ExternalDocumentID | PMC11157532 38789103 10_1021_acs_jafc_4c00974 c655388378 |
| Genre | Journal Article |
| GroupedDBID | --- -~X .K2 4.4 55A 5GY 5VS 7~N 85S AABXI AAHBH ABFRP ABJNI ABMVS ABQRX ABUCX ACGFO ACGFS ACJ ACS ADHLV AEESW AENEX AFEFF AGXLV AHGAQ ALMA_UNASSIGNED_HOLDINGS AQSVZ BAANH CS3 CUPRZ DU5 EBS ED~ F5P GGK GNL GX1 IH9 JG~ LG6 P2P ROL TWZ UI2 VF5 VG9 W1F WH7 ABBLG ABLBI RYH AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 7S9 L.6 5PM |
| ID | FETCH-LOGICAL-a606t-532cc2bfbb0d56b789c029dd7b9c66382be6e1ebacd48d4450d18ba521f946683 |
| IEDL.DBID | ACS |
| ISSN | 0021-8561 1520-5118 |
| IngestDate | Thu Aug 21 18:33:44 EDT 2025 Fri Jul 11 15:47:54 EDT 2025 Thu Jul 10 18:26:53 EDT 2025 Mon Jul 21 05:59:17 EDT 2025 Tue Jul 01 01:40:39 EDT 2025 Thu Apr 24 23:07:05 EDT 2025 Thu Jun 26 21:19:12 EDT 2025 Tue Jun 25 16:50:43 EDT 2024 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 22 |
| Keywords | lactononadecapeptide (LNDP) intestinal transport peptide Caco-2 cells beta-casein peptide transporter 1 (PEPT1) |
| Language | English |
| License | https://creativecommons.org/licenses/by-nc-nd/4.0 Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-a606t-532cc2bfbb0d56b789c029dd7b9c66382be6e1ebacd48d4450d18ba521f946683 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| ORCID | 0009-0001-8095-5450 |
| OpenAccessLink | https://pubmed.ncbi.nlm.nih.gov/PMC11157532 |
| PMID | 38789103 |
| PQID | 3060373180 |
| PQPubID | 23479 |
| PageCount | 6 |
| ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_11157532 proquest_miscellaneous_3153613824 proquest_miscellaneous_3060373180 pubmed_primary_38789103 crossref_primary_10_1021_acs_jafc_4c00974 crossref_citationtrail_10_1021_acs_jafc_4c00974 nii_cinii_1873399491341085952 acs_journals_10_1021_acs_jafc_4c00974 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2024-06-05 |
| PublicationDateYYYYMMDD | 2024-06-05 |
| PublicationDate_xml | – month: 06 year: 2024 text: 2024-06-05 day: 05 |
| PublicationDecade | 2020 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States |
| PublicationTitle | Journal of Agricultural and Food Chemistry |
| PublicationTitleAlternate | J. Agric. Food Chem |
| PublicationYear | 2024 |
| Publisher | American Chemical Society American Chemical Society (ACS) |
| Publisher_xml | – name: American Chemical Society – name: American Chemical Society (ACS) |
| References | ref9/cit9 ref45/cit45 ref3/cit3 ref27/cit27 ref16/cit16 ref8/cit8 ref31/cit31 ref2/cit2 ref34/cit34 ref37/cit37 ref20/cit20 ref48/cit48 Nakamura F. (ref26/cit26) 2018; 95 ref17/cit17 ref10/cit10 ref35/cit35 ref19/cit19 ref21/cit21 ref42/cit42 ref46/cit46 ref49/cit49 ref13/cit13 Nakamura F. (ref23/cit23) 2017; 45 ref24/cit24 ref38/cit38 ref6/cit6 ref36/cit36 ref18/cit18 ref11/cit11 ref25/cit25 ref29/cit29 ref32/cit32 ref39/cit39 ref14/cit14 ref5/cit5 ref43/cit43 ref28/cit28 ref40/cit40 ref12/cit12 ref15/cit15 ref41/cit41 ref22/cit22 ref33/cit33 ref4/cit4 ref30/cit30 ref47/cit47 ref1/cit1 ref44/cit44 ref7/cit7 |
| References_xml | – ident: ref10/cit10 doi: 10.1017/S0954422416000032 – ident: ref35/cit35 doi: 10.1021/acs.jcim.1c00380 – ident: ref49/cit49 doi: 10.1002/jps.20075 – ident: ref25/cit25 – volume: 95 start-page: 9 year: 2018 ident: ref26/cit26 publication-title: Pharmacometrics – ident: ref19/cit19 doi: 10.1016/0006-291X(91)91647-U – ident: ref38/cit38 doi: 10.3390/molecules24152843 – ident: ref12/cit12 doi: 10.1002/psc.870 – ident: ref2/cit2 doi: 10.1016/j.bbrc.2018.06.118 – ident: ref41/cit41 doi: 10.1016/j.coph.2013.08.004 – ident: ref32/cit32 doi: 10.1021/pr0705035 – ident: ref39/cit39 doi: 10.1002/mnfr.200700503 – ident: ref29/cit29 doi: 10.1021/jf703640p – ident: ref24/cit24 doi: 10.1093/bbb/zbaa117 – ident: ref11/cit11 doi: 10.1038/368563a0 – ident: ref47/cit47 doi: 10.1016/j.ajps.2018.05.008 – ident: ref28/cit28 doi: 10.1021/acs.jafc.7b02176 – ident: ref44/cit44 doi: 10.1021/acs.jafc.3c04940 – volume: 45 start-page: 1303 issue: 8 year: 2017 ident: ref23/cit23 publication-title: Jpn. Pharmacol Ther. – ident: ref46/cit46 doi: 10.3390/molecules28031151 – ident: ref16/cit16 doi: 10.1016/0016-5085(89)90897-4 – ident: ref48/cit48 doi: 10.1007/s11095-005-6156-9 – ident: ref30/cit30 doi: 10.1016/0005-2744(74)90053-9 – ident: ref33/cit33 doi: 10.1152/ajpgi.00136.2002 – ident: ref45/cit45 doi: 10.1074/jbc.273.7.3861 – ident: ref20/cit20 doi: 10.1179/1476830514Y.0000000122 – ident: ref4/cit4 doi: 10.1016/j.peptides.2022.170843 – ident: ref42/cit42 doi: 10.1016/j.foodchem.2015.05.121 – ident: ref14/cit14 doi: 10.1083/jcb.102.6.2125 – ident: ref7/cit7 doi: 10.1002/psc.371 – ident: ref15/cit15 doi: 10.1074/jbc.270.47.28425 – ident: ref34/cit34 doi: 10.1271/bbb.66.378 – ident: ref9/cit9 doi: 10.1039/b301507f – ident: ref21/cit21 doi: 10.1080/09637486.2017.1324564 – ident: ref3/cit3 doi: 10.3168/jds.S0022-0302(96)76585-2 – ident: ref27/cit27 doi: 10.1021/acs.jafc.1c08191 – ident: ref18/cit18 doi: 10.1002/mnfr.200900443 – ident: ref1/cit1 doi: 10.3168/jds.S0022-0302(95)76745-5 – ident: ref36/cit36 doi: 10.1021/jf405639w – ident: ref40/cit40 doi: 10.3390/pharmaceutics15102517 – ident: ref8/cit8 doi: 10.3168/jds.S0022-0302(04)73453-0 – ident: ref22/cit22 doi: 10.1080/09637486.2017.1365824 – ident: ref13/cit13 doi: 10.1002/(SICI)1521-3803(19990601)43:3<154::AID-FOOD154>3.0.CO;2-A – ident: ref31/cit31 doi: 10.1002/0471140864.ps2103s25 – ident: ref6/cit6 doi: 10.1096/fj.201900621R – ident: ref43/cit43 doi: 10.1016/j.jff.2017.06.001 – ident: ref17/cit17 doi: 10.1042/bj2840595 – ident: ref5/cit5 doi: 10.1016/j.neurobiolaging.2018.07.016 – ident: ref37/cit37 doi: 10.1021/acs.jafc.5b01824 |
| SSID | ssj0008570 ssib000630454 ssib017385285 ssib045322535 ssib000983874 ssib045322530 ssib006542241 |
| Score | 2.4668384 |
| Snippet | Lactononadecapeptide (LNDP; NIPPLTQTPVVVPPFLQPE), a casein-derived peptide comprising 19 residues, is known for its capacity to enhance cognitive... Lactononadecapeptide (LNDP; NIPPLTQTPVVVPPFLQPE), a casein-derived peptide comprising 19 residues, is known for its capacity to enhance cognitive function.... Lactononadecapeptide (LNDP; NIPPLTQTPVVVPPFLQPE), a casein-derived peptide comprising 19 residues, is known for its capacity to enhance cognitive function.... |
| SourceID | pubmedcentral proquest pubmed crossref nii acs |
| SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 12719 |
| SubjectTerms | Biological Transport Caco-2 Cells Caseins - chemistry Caseins - genetics Caseins - metabolism cognition Enzyme Stability Food and Beverage Chemistry/Biochemistry food chemistry human cell lines Humans intestinal mucosa Intestinal Mucosa - metabolism lipids Peptide Transporter 1 - genetics Peptide Transporter 1 - metabolism peptide transporters peptides Peptides - chemistry Peptides - metabolism permeability |
| Title | Investigating the Transepithelial Transport and Enzymatic Stability of Lactononadecapeptide (NIPPLTQTPVVVPPFLQPE), a 19-Amino Acid Casein-Derived Peptide in Caco‑2 Cells |
| URI | http://dx.doi.org/10.1021/acs.jafc.4c00974 https://cir.nii.ac.jp/crid/1873399491341085952 https://www.ncbi.nlm.nih.gov/pubmed/38789103 https://www.proquest.com/docview/3060373180 https://www.proquest.com/docview/3153613824 https://pubmed.ncbi.nlm.nih.gov/PMC11157532 |
| Volume | 72 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjZ3dbtMwFMctNm7ggu-PAkNGAolJpIudxHEuq9JqoDJ1oqt2F_krI1DcaWmRtitegQfpNfd9FJ6EYzcr65iq3VRp4ziNfXzO3_LJzwi9Br8oMx6ZQHKjg5hFNBBZzAJqMpWwKGbM0_Y_7bHdg_jjYXL4D5NzeQWfkh2hquZXUahmrNxLB_EGukkZT91Eq9X-vPS6DtS-SOcgAQdRUC9JXlWDC0SqWglEG7Ysr9KYl1MlL8Se7t3FJkaVRxa6lJNvzelENtXZ_0DHazzWPXSnlqC4tbCZ--iGsQ_Q7dbRSY3hMA_R7wv4DXuEQSRiH9TMsXuFYwQ2i5dUdCysxh17durhrxjUq8-3PcXjAvfcbj4WxL42LtEK3JM2-O3eh_581u8N5rP9ARwNh0P42u_OZ719OOhsv8MCkyxofS_tGLdUqXEbYm1pg_cwXH4Yjft1TaWFM2r85-cvittmNKoeoYNuZ9DeDeotHgIBM6dJkERUKSoLKUOdMJnyTIU00zqVmQItxKk0zBAjhdIx13GchJpwKUBzFA6Mz6PHaBOewjxFmAoppYiILhgFr6RlkabcpDLVnCSSsgZ6A22e10O0yv3qOyW5_xE6Iq87ooF2zu0iVzUn3W3XMVpzxfbyiuMFI2RN2S0wNajYfRKeRiAQY5f9QDxpjjbQq3MjzGGgu9UbYc14WuUwtwujFFxwuKYMxC_mqJJwnycLw13-o4hD65IwaiC-YtLLAg40vnrGll88cJw4IhN01bNrNuFzdIuC9vMZdckLtDk5mZot0G4T-dIP2r_lykNB |
| linkProvider | American Chemical Society |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1bb9MwFLa28QA8cL8UGBgJJCaRLnYSx3msSqsOuqqDrtpbFF8yAiWdlhZpe-Iv8EP6zHt_Cr-EYzcN6zRV8BI5tuP4cnzOZ_n4M0KvQC-KiHvaEVwrx2cedZLIZw7VkQyY5zNm2fb3e6xz6L8_Co42EFmehYFKFFBSYTfx_7ILkF0T9yVJZd2X5uyBv4muARahZr3VaH6qlK_ha194dRCHAzYodyavKsHYI1ms2KPNPMuugpqXPSYvmKD2bfSxqrz1PPlan05EXZ5f4nX8r9bdQbdKQIobCwm6izZ0fg_dbByflqQc-j76dYGMIz_GABmxNXH6xBzoGIEE44ojHSe5wq38_MxSwWLAstb79gyPU9w1d_vkAP2VNm5XoKyUxm96e_35rN8dzGcHAwgNh0N47bfns-4BBFo7b3GCSeQ0vmX5GDdkpnATLG-WO-9g8nzXCvfLkrIcUuT494-fFDf1aFQ8QIft1qDZccoLH5wE1lETJ_ColFSkQrgqYCLkkXRppFQoIgnIiFOhmSZaJFL5XPl-4CrCRQIIJDU0-dx7iLagFfoxwjQRQiQeUSmjoKOUSMOQ61CEipNAUFZDr6HP43LCFrHdi6cktpEwEHE5EDW0uxSPWJas6ebyjtGaL3aqL04WjCFr8m6DxEHB5kl46AFc9I0vBLG8c7SGXi5lMYZpb_ZyklyPp0UMKz3XC0Ehu2vygDVjhmMS_vNoIb9VjTwOvUtcr4b4imRXGQzt-GpKnn229OPE8DPBUD35xy58ga53BvvduLvX-_AU3aCACq2vXfAMbU1Op3obUN1EPLfz-A_z-Uui |
| linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV3bbtMwGLa2ISG44HwoMDASSEwiXewkjnNZda02KFUnump3UXzIllHSammRtitegQfpNfd9FJ6E324ardNUwU2Ug-PE9n_4rP_3Z4TegV0UEfe0I7hWjs886iSRzxyqIxkwz2fMsu1_6bL9I__TcXC8gYLlWhj4iQJqKmwQ32j1WKUlwwDZNffPklTWfWnWH_ib6JaJ2pk5V6P5tTLAhrN9kdlBHA74oIxO3lSD8UmyWPFJm3mW3QQ3r2dNXnFD7ftoUDXAZp98q08noi4vr3E7_ncLH6B7JTDFjYUkPUQbOn-E7jZOzktyDv0Y_b5CypGfYICO2Lo6PTYLO4YgybjiSsdJrnArv7ywlLAYMK3Nwr3AoxR3zB4_OUwBlDbpV2C0lMYfuge9-azX6c9nh304GwwGcNlrz2edQzhp7XzECSaR0_ie5SPckJnCTfDAWe7sgRL90Ar3ypqyHJ7I0Z-fvyhu6uGweIKO2q1-c98pN35wEphPTZzAo1JSkQrhqoCJkEfSpZFSoYgkICROhWaaaJFI5XPl-4GrCBcJIJHU0OVz7ynaglbo5wjTRAiReESljIKtUiINQ65DESpOAkFZDb2HPo9LxS1iG5OnJLY3YSDiciBqaHcpIrEs2dPNJh7DNW_sVG-MF8wha8pug9RBxeZIeOgBbPRNTgSx_HO0ht4u5TEG9TcxnSTXo2kRw4zP9UIwzO6aMuDVmOGahO88W8hw9Uceh94lrldDfEW6qwKGfnz1SZ6dWhpyYniaYKhe_GMXvkG3e3vtuHPQ_fwS3aEADm3KXfAKbU3Op3obwN1EvLaq_BdPr04l |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Investigating+the+Transepithelial+Transport+and+Enzymatic+Stability+of+Lactononadecapeptide+%28NIP%C2%ADPLT%C2%ADQTP%C2%ADVVV%C2%ADPPF%C2%ADLQ%C2%ADPE%29%2C+a+19-Amino+Acid+Casein-Derived+Peptide+in+Caco%E2%80%912+Cells&rft.jtitle=Journal+of+agricultural+and+food+chemistry&rft.au=Nakatani%2C+Eriko&rft.au=Sasai%2C+Masaki&rft.au=Miyazaki%2C+Hidetoshi&rft.au=Tanaka%2C+Shimako&rft.date=2024-06-05&rft.issn=1520-5118&rft.volume=72&rft.issue=22+p.12719-12724&rft.spage=12719&rft.epage=12724&rft_id=info:doi/10.1021%2Facs.jafc.4c00974&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0021-8561&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0021-8561&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0021-8561&client=summon |