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Intrinsic Reactivities of Amino Acids towards Photoalkylation with Benzophenone − A Study Preliminary to Photolabelling of the Transmembrane Protein Glycophorin A
Author(s) -
Deseke Eckart,
Nakatani Yoichi,
Ourisson Guy
Publication year - 1998
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/(sici)1099-0690(199802)1998:2<243::aid-ejoc243>3.0.co;2-i
Subject(s) - chemistry , amino acid , glycophorin , benzophenone , reactivity (psychology) , glycine , lability , transmembrane protein , methionine , stereochemistry , organic chemistry , membrane , biochemistry , receptor , medicine , alternative medicine , pathology
A systematic study of the photoalkylation of amino acids by benzophenone, a standard photosensitive probe of biomolecules, was performed addressing for the first time chemo‐, regio‐, and stereoselectivities. The high reactivity of the capto‐dative substituted α‐carbon, particularly in glycine, could be demonstrated as well as the chemical lability of the α‐coupling products. Methionine was shown to be favoured both in the sense of reactivity as well as product stability. Preliminary to a project directed towards the elucidation of the topography of glycophorin A in membranes, the present model experiments focussed on the ten amino acids that constitute the transmembrane part of this protein.