Abstract
Two protected peptides Boc-Val-Ser(Bzl)-Gln-Asn-Tyr(BrZ)OH and Boc-Val-Ser(Bzl)-Gln-Asn-Tyr(BrZ)-ProOH were synthesized on a resin substituted by 9-(hydroxymethyl)-2-fluoreneacetic acid. After cleavage with piperidine/DMF, desalting, and activation, these peptides were used for the synthesis of 11 analogs of an HIV proteinase nonapeptide substrate Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln-NH2 using fragment condensation in solid phase. The fragment condensation was made in an ultrasonic bath. Using only 2 equivalents of the activated peptide in a DMF solution, this reaction was complete in 2 h. All nonapeptides were assayed as substrates for HIV-1 and HIV-2 proteinases.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Aspartic Acid Endopeptidases
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Dimethylformamide / chemistry
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HIV Protease / metabolism*
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Molecular Sequence Data
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Oligopeptides / chemical synthesis*
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Oligopeptides / chemistry
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Oligopeptides / metabolism
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Sequence Homology, Nucleic Acid
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Structure-Activity Relationship
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Substrate Specificity
Substances
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Oligopeptides
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tert-butyloxycarbonyl-valyl-benzylseryl-glutaminyl-asparaginyl-(BrZ)tyrosine
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tert-butyloxycarbonyl-valyl-(benzyl)seryl-glutaminyl-asparaginyl-(BrZ)tyrosyl-proline
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HIV protease nonapeptide substrate
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Dimethylformamide
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Aspartic Acid Endopeptidases
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HIV Protease
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p16 protease, Human immunodeficiency virus 2