Asteropsins B–D, sponge-derived knottins with potential utility as a novel scaffold for oral peptide drugs
Known linear knottins are unsuitable as scaffolds for oral peptide drug due to their gastrointestinal instability. Herein, a new subclass of knottin peptides from Porifera is structurally described and characterized regarding their potential for oral peptide drug development. Asteropsins B–D (ASPB,...
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| Published in | Biochimica et biophysica acta Vol. 1840; no. 3; pp. 977 - 984 |
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| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
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Netherlands
Elsevier B.V
01.03.2014
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| Abstract | Known linear knottins are unsuitable as scaffolds for oral peptide drug due to their gastrointestinal instability. Herein, a new subclass of knottin peptides from Porifera is structurally described and characterized regarding their potential for oral peptide drug development.
Asteropsins B–D (ASPB, ASPC, and ASPD) were isolated from the marine sponge Asteropus sp. The tertiary structures of ASPB and ASPC were determined by solution NMR spectroscopy and that of ASPD by homology modeling.
The isolated asteropsins B–D, together with the previously reported asteropsin A (ASPA), compose a new subclass of knottins that share a highly conserved structural framework and remarkable stability against the enzymes in gastrointestinal tract (chymotrypsin, elastase, pepsin, and trypsin) and human plasma.
Asteropsins can be considered as promising peptide scaffolds for oral bioavailability.
The structural details of asteropsins provide essential information for the engineering of orally bioavailable peptides.
•An unusual subclass of knottin peptides from a sponge•Peptides share highly conserved structural framework.•Solution NMR structures were analyzed in detail.•Showed remarkable stability against key gastrointestinal enzymes•Potential scaffold for oral peptide drugs |
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| AbstractList | Known linear knottins are unsuitable as scaffolds for oral peptide drug due to their gastrointestinal instability. Herein, a new subclass of knottin peptides from Porifera is structurally described and characterized regarding their potential for oral peptide drug development.
Asteropsins B–D (ASPB, ASPC, and ASPD) were isolated from the marine sponge Asteropus sp. The tertiary structures of ASPB and ASPC were determined by solution NMR spectroscopy and that of ASPD by homology modeling.
The isolated asteropsins B–D, together with the previously reported asteropsin A (ASPA), compose a new subclass of knottins that share a highly conserved structural framework and remarkable stability against the enzymes in gastrointestinal tract (chymotrypsin, elastase, pepsin, and trypsin) and human plasma.
Asteropsins can be considered as promising peptide scaffolds for oral bioavailability.
The structural details of asteropsins provide essential information for the engineering of orally bioavailable peptides.
•An unusual subclass of knottin peptides from a sponge•Peptides share highly conserved structural framework.•Solution NMR structures were analyzed in detail.•Showed remarkable stability against key gastrointestinal enzymes•Potential scaffold for oral peptide drugs Known linear knottins are unsuitable as scaffolds for oral peptide drug due to their gastrointestinal instability. Herein, a new subclass of knottin peptides from Porifera is structurally described and characterized regarding their potential for oral peptide drug development.Asteropsins B–D (ASPB, ASPC, and ASPD) were isolated from the marine sponge Asteropus sp. The tertiary structures of ASPB and ASPC were determined by solution NMR spectroscopy and that of ASPD by homology modeling.The isolated asteropsins B–D, together with the previously reported asteropsin A (ASPA), compose a new subclass of knottins that share a highly conserved structural framework and remarkable stability against the enzymes in gastrointestinal tract (chymotrypsin, elastase, pepsin, and trypsin) and human plasma.Asteropsins can be considered as promising peptide scaffolds for oral bioavailability.The structural details of asteropsins provide essential information for the engineering of orally bioavailable peptides. Known linear knottins are unsuitable as scaffolds for oral peptide drug due to their gastrointestinal instability. Herein, a new subclass of knottin peptides from Porifera is structurally described and characterized regarding their potential for oral peptide drug development.BACKGROUNDKnown linear knottins are unsuitable as scaffolds for oral peptide drug due to their gastrointestinal instability. Herein, a new subclass of knottin peptides from Porifera is structurally described and characterized regarding their potential for oral peptide drug development.Asteropsins B-D (ASPB, ASPC, and ASPD) were isolated from the marine sponge Asteropus sp. The tertiary structures of ASPB and ASPC were determined by solution NMR spectroscopy and that of ASPD by homology modeling.METHODSAsteropsins B-D (ASPB, ASPC, and ASPD) were isolated from the marine sponge Asteropus sp. The tertiary structures of ASPB and ASPC were determined by solution NMR spectroscopy and that of ASPD by homology modeling.The isolated asteropsins B-D, together with the previously reported asteropsin A (ASPA), compose a new subclass of knottins that share a highly conserved structural framework and remarkable stability against the enzymes in gastrointestinal tract (chymotrypsin, elastase, pepsin, and trypsin) and human plasma.RESULTSThe isolated asteropsins B-D, together with the previously reported asteropsin A (ASPA), compose a new subclass of knottins that share a highly conserved structural framework and remarkable stability against the enzymes in gastrointestinal tract (chymotrypsin, elastase, pepsin, and trypsin) and human plasma.Asteropsins can be considered as promising peptide scaffolds for oral bioavailability.CONCLUSIONAsteropsins can be considered as promising peptide scaffolds for oral bioavailability.The structural details of asteropsins provide essential information for the engineering of orally bioavailable peptides.GENERAL SIGNIFICANCEThe structural details of asteropsins provide essential information for the engineering of orally bioavailable peptides. Known linear knottins are unsuitable as scaffolds for oral peptide drug due to their gastrointestinal instability. Herein, a new subclass of knottin peptides from Porifera is structurally described and characterized regarding their potential for oral peptide drug development. Asteropsins B-D (ASPB, ASPC, and ASPD) were isolated from the marine sponge Asteropus sp. The tertiary structures of ASPB and ASPC were determined by solution NMR spectroscopy and that of ASPD by homology modeling. The isolated asteropsins B-D, together with the previously reported asteropsin A (ASPA), compose a new subclass of knottins that share a highly conserved structural framework and remarkable stability against the enzymes in gastrointestinal tract (chymotrypsin, elastase, pepsin, and trypsin) and human plasma. Asteropsins can be considered as promising peptide scaffolds for oral bioavailability. The structural details of asteropsins provide essential information for the engineering of orally bioavailable peptides. |
| Author | Bowling, John J. Jung, Jee H. Li, Huayue Lee, Bong-Jin Hong, Jongki Su, Mingzhi Hamann, Mark T. |
| AuthorAffiliation | c College of Pharmacy, Kyung Hee University, Seoul 130-701, Republic of Korea d College of Pharmacy, Seoul National University, Seoul 151-742, Republic of Korea a College of Pharmacy, Pusan National University, Busan 609-735, Republic of Korea b Department of Pharmacognosy, School of Pharmacy, The University of Mississippi, Oxford, MN 38677, USA |
| AuthorAffiliation_xml | – name: a College of Pharmacy, Pusan National University, Busan 609-735, Republic of Korea – name: d College of Pharmacy, Seoul National University, Seoul 151-742, Republic of Korea – name: c College of Pharmacy, Kyung Hee University, Seoul 130-701, Republic of Korea – name: b Department of Pharmacognosy, School of Pharmacy, The University of Mississippi, Oxford, MN 38677, USA |
| Author_xml | – sequence: 1 givenname: Huayue surname: Li fullname: Li, Huayue email: lihuayue@naver.com organization: College of Pharmacy, Pusan National University, Busan 609-735, Republic of Korea – sequence: 2 givenname: John J. surname: Bowling fullname: Bowling, John J. email: bowlingjj@gmail.com organization: Department of Pharmacognosy, School of Pharmacy, The University of Mississippi, Oxford, MN 38677, USA – sequence: 3 givenname: Mingzhi surname: Su fullname: Su, Mingzhi email: smz0310@163.com organization: College of Pharmacy, Pusan National University, Busan 609-735, Republic of Korea – sequence: 4 givenname: Jongki surname: Hong fullname: Hong, Jongki email: jhong@khu.ac.kr organization: College of Pharmacy, Kyung Hee University, Seoul 130-701, Republic of Korea – sequence: 5 givenname: Bong-Jin surname: Lee fullname: Lee, Bong-Jin email: lbj@nmr.snu.ac.kr organization: College of Pharmacy, Seoul National University, Seoul 151-742, Republic of Korea – sequence: 6 givenname: Mark T. surname: Hamann fullname: Hamann, Mark T. email: mthamann@olemiss.edu organization: Department of Pharmacognosy, School of Pharmacy, The University of Mississippi, Oxford, MN 38677, USA – sequence: 7 givenname: Jee H. surname: Jung fullname: Jung, Jee H. email: jhjung@pusan.ac.kr organization: College of Pharmacy, Pusan National University, Busan 609-735, Republic of Korea |
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| CitedBy_id | crossref_primary_10_1021_np400899a crossref_primary_10_1016_j_bmc_2016_05_006 crossref_primary_10_1371_journal_pone_0299804 crossref_primary_10_1021_jacs_0c10418 crossref_primary_10_1002_slct_202401844 crossref_primary_10_1021_acs_joc_4c01104 crossref_primary_10_1146_annurev_anchem_061516_045205 crossref_primary_10_2174_1389557517666170927113143 crossref_primary_10_1039_C5NP00156K crossref_primary_10_1155_2015_537508 |
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| Keywords | Marine sponge NMR Knottin Asteropus sp Oral peptide drug delivery Solution structure |
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| Snippet | Known linear knottins are unsuitable as scaffolds for oral peptide drug due to their gastrointestinal instability. Herein, a new subclass of knottin peptides... |
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| SubjectTerms | Administration, Oral Amino Acid Sequence Animals Asteropus sp Calcium - metabolism chymotrypsin Cystine-Knot Miniproteins - chemistry Drug Discovery drugs elastase engineering gastrointestinal system humans Knottin Marine sponge Models, Molecular Molecular Sequence Data NMR nuclear magnetic resonance spectroscopy Oral peptide drug delivery pepsin peptides Porifera Porifera - chemistry Protein Stability Protein Structure, Secondary Protein Structure, Tertiary Solution structure trypsin |
| Title | Asteropsins B–D, sponge-derived knottins with potential utility as a novel scaffold for oral peptide drugs |
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