NDLI: Chemical synthesis, structure–activity relationship, and properties of shepherin I: a fungicidal peptide enriched in glycine-glycine-histidine motifs

Content Provider	Springer Nature Link
Author	Remuzgo, César Oewel, Thaís S. Daffre, Sirlei Lopes, Thiago R. S. Dyszy, Fabio H. Schreier, Shirley Machado Santelli, Gláucia M. Teresa Machini, M.
Copyright Year	2014
Abstract	Although glycine-rich antimicrobial peptides (AMPs) are found in animals and plants, very little has been reported on their chemistry, structure activity-relationship, and properties. We investigated those topics for Shepherin I (Shep I), a glycine-rich AMP with the unique amino acid sequence G1YGGHGGHGGHGGHGGHGGHGHGGGGHG28. Shep I and analogues were synthesized by the solid-phase method at 60 °C using conventional heating. Purification followed by chemical characterization confirmed the products' identities and high purity. Amino acid analysis provided their peptide contents. All peptides were active against the clinically important Candida species, but ineffective against bacteria and mycelia fungi. Truncation of the N- or C-terminal portion reduced Shep I antifungal activity, the latter being more pronounced. Carboxyamidation of Shep I did not affect the activity against C. albicans or C. tropicalis, but increased activity against S. cerevisiae. Carboxyamidated analogues Shep I (3-28)a and Shep I (6-28)a were equipotent to Shep I and Shep Ia against Candida species. As with most cationic AMPs, all peptides had their activity significantly reduced in high-salt concentrations, a disadvantage that is defeated if 10 µM ZnCl2 is present. At 100 µM, the peptides were practically not hemolytic. Shep Ia also killed C. albicans MDM8 and ATCC 90028 cells. Fluo-Shep Ia, an analogue labeled with 5(6)-carboxyfluorescein, was rapidly internalized by C. albicans MDM8 cells, a salt-sensitive process dependent on metabolic energy and temperature. Altogether, such results shed light on the chemistry, structural requirements for activity, and other properties of candidacidal glycine-rich peptides. Furthermore, they show that Shep Ia may have strong potential for use in topical application.
Starting Page	2573
Ending Page	2586
Page Count	14
File Format	PDF
ISSN	09394451
Journal	Amino Acids
Volume Number	46
Issue Number	11
e-ISSN	14382199
Language	English
Publisher	Springer Vienna
Publisher Date	2014-08-09
Publisher Place	Vienna
Access Restriction	Subscribed
Subject Keyword	Synthesis at 60 °C Antimicrobial peptide Fungicidal activity Structure–activity relationship Biochemistry Analytical Chemistry Biochemical Engineering Life Sciences Proteomics Neurobiology
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Clinical Biochemistry

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