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chassalia curviflora/cistein
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New circulin macrocyclic polypeptides from Chassalia parvifolia.
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Four new macrocyclic polypeptides were isolated and identified from an extract of the tropical tree Chassalia parvifolia. Circulins C-F are 29-30 amino acid cyclic peptides in which the entire primary amino acid chain is covalently cyclized via peptide bonds. Their structures were deduced from a
Analysis of the disulfide linkage pattern in circulin A and B, HIV-inhibitory macrocyclic peptides.
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Circulin A and B are members of a family of macrocyclic peptides, originally isolated from the tropical tree Chassalia parvifolia, that have been shown to display anti-HIV activity. Complete structural elucidation of these highly constrained peptides was difficult due to their cyclic amide backbone
Solution structure by NMR of circulin A: a macrocyclic knotted peptide having anti-HIV activity.
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The three-dimensional solution structure of circulin A, a 30 residue polypeptide from the African plant Chassalia parvifolia, has been determined using two-dimensional 1H-NMR spectroscopy. Circulin A was originally identified based upon its inhibition of the cytopathic effects and replication of the
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