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PubMed · 697739

A structural model for desmosine cross-linked peptides.

R P Mecham·J A Foster
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Abstract

Desmosine-enriched peptides were isolated from a thermolysin digest of bovine ligamentum nuchae elastin and a partial sequence was determined. A 'two-cross-link' model is proposed in which a second cross-link, perhaps lysinonorleucine, joins two peptide chains approx. 35 amino acid residues removed from the desmosine. Implied in this model is a certain asymmetry or directionality which places restrictions on the 'sense' of the peptide chains (either always parallel or anti-parallel) in order to align the cross-linking sites. Imposing such restrictions raises the possibility of specific alignment of elastin precursor molecules by microfibrillar proteins and/or aligning peptides on the precursor molecules themselves.

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Amino Acid SequenceChromatography, Ion ExchangeDesmosineElastinModels, MolecularPeptide FragmentsThermolysinJournal ArticleResearch Support, U.S. Gov't, P.H.S.

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R P Mecham, J A Foster. 1978-08-01. A structural model for desmosine cross-linked peptides.. https://doi.org/10.1042/bj1730617

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