Abstract
Two linear peptides, ahpatinin Ac (1) and ahpatinin Pr (2), were isolated together with the known ahpatinin (i)Bu, pepstatin Ac, pepstatin Pr, and pepsinostreptin from a Streptomyces sp. derived from a deep-sea sediment. The structure of ahpatinin Pr (2) was assigned by interpretation of NMR data and HPLC analysis of the hydrolysate after converting to the DNP-L-Val derivative. During the LCMS analysis of the acid hydrolysate, products arising from the retro-aldol cleavage of the statine and Ahppa units in 2 were observed and could facilitate the determination of the absolute configuration of the statine class of nonproteinogenic amino acids. Both ahpatinin Ac (1) and ahpatinin Pr (2) potently inhibited pepsin and moderately inhibited cathepsin B.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acids / chemistry
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Aspartic Acid Endopeptidases / antagonists & inhibitors*
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Cathepsin B / antagonists & inhibitors
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Marine Biology
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Molecular Structure
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Oligopeptides / chemistry
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Oligopeptides / isolation & purification*
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Oligopeptides / pharmacology*
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Pepsin A / antagonists & inhibitors
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Pepstatins / chemistry
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Pepstatins / isolation & purification*
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Pepstatins / pharmacology*
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Protease Inhibitors / chemistry
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Protease Inhibitors / isolation & purification*
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Protease Inhibitors / pharmacology*
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Streptomyces / chemistry*
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Structure-Activity Relationship
Substances
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Amino Acids
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Oligopeptides
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Pepstatins
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Protease Inhibitors
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Streptomyces pepsin inhibitor
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pepsinostreptin
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Cathepsin B
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Aspartic Acid Endopeptidases
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Pepsin A
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pepstatin
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statine