Contribution of cationic amino acids toward the inhibition of Arg-specific cysteine proteinase (Arg-gingipain) by the antimicrobial dodecapeptide, CL(14-25), from rice protein

ABSTRACT CL(14–25), a dodecapeptide, exhibits antimicrobial activity against Porphyromonas gingivalis with the 50% growth‐inhibitory concentration (IC50) value of 145 µM, and arginine‐specific gingipain (Rgp)‐inhibitory activity. Kinetic analysis revealed that CL(14–25) is a mixed‐type inhibitor, wi...

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Published inBiopolymers Vol. 102; no. 5; pp. 379 - 389
Main Authors Taniguchi, Masayuki, Matsuhashi, Yoshiyasu, Abe, Takako K., Ishiyama, Yohei, Saitoh, Eiichi, Kato, Tetsuo, Ochiai, Akihito, Tanaka, Takaaki
Format Journal Article
LanguageEnglish
Published United States Blackwell Publishing Ltd 01.09.2014
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Summary:ABSTRACT CL(14–25), a dodecapeptide, exhibits antimicrobial activity against Porphyromonas gingivalis with the 50% growth‐inhibitory concentration (IC50) value of 145 µM, and arginine‐specific gingipain (Rgp)‐inhibitory activity. Kinetic analysis revealed that CL(14–25) is a mixed‐type inhibitor, with inhibition constants (Ki and Ki′ values) of 1.4 × 10−6 M and 4.3 × 10−6 M, respectively. To elucidate the contributions of four cationic amino acid residues at the N‐ and C‐termini of CL(14–25) toward Rgp‐inhibitory activity, we investigated the Rgp‐inhibitory activities of truncated and alanine‐substituted analogs of CL(14–25). Rgp‐inhibitory activities significantly decreased by truncated analogs, CL(15–25) and CL(16–25), whereas those of CL(14–24) and CL(14–23) were almost as high as that of CL(14–25). Rgp‐inhibitory activities of alanine‐substituted analogs, CL(R14A) and CL(R14A, R15A) also significantly decreased, whereas those of CL(K25A) and CL(R24A, K25A) were higher than that of CL(14–25). These results suggest that the arginine residue at position 15 substantially contributes to the Rgp‐inhibitory activity and that the arginine residue at position 14 plays important roles in exerting Rgp‐inhibitory activity. In this study, we demonstrated that CL(K25A) was a potent, dual function, peptide inhibitor candidate, exhibiting Rgp‐inhibitory activity with Ki and Ki′ of 9.6 × 10−7 M and 1.9 × 10−6 M, respectively, and antimicrobial activity against P. gingivalis with an IC50 value of 51 µM. © 2014 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 102: 379–389, 2014.
Bibliography:ark:/67375/WNG-4CXKL3S5-B
ArticleID:BIP22525
KAKENHI, the Ministry of Education, Culture, Sports, Science and Technology of Japan - No. 23560939
istex:42A79DE863FF8B942F1E522C3649D338F183F4DD
Development of Fundamental Technology for Analysis and Evaluation of Functional Agricultural Products and Functional Foods
This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of any preprints from the past two calendar years by emailing the Biopolymers editorial office at
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biopolymers@wiley.com
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-3525
1097-0282
DOI:10.1002/bip.22525