RESUMO
Sense peptides and corresponding antisense peptides, are capable of making specific interactions. Such interactions may result from inter-peptide side-chain/side-chain contacts or because peptides adopt mutually complementary three-dimensional shapes. Using a combined (1)H NMR spectroscopy/molecular modeling approach to study the interactions between one sense peptide and its corresponding antisense peptide, data are produced that provide clear support for the former hypothesis.
Assuntos
Modelos Moleculares , Peptídeos/química , Elementos Antissenso (Genética)/química , Espectroscopia de Ressonância Magnética , Conformação Molecular , Simulação de Dinâmica MolecularRESUMO
Controlled protein folding/refolding remains a substantial challenge to the biotechnology industry. Robust and adaptable artificial polymer molecular chaperones could make important contributions towards solving this problem. Taking inspiration from the mechanism of the GroEL/GroES molecular chaperone machine, we report the preparation and testing of a selection of cross-linked thermo-responsive hydrogels, one of which is shown to assist quantitative refolding of a stringent unfolded protein substrate (mitochondrial malate dehydrogenase [mMDH]) during temperature cycling between hydrophobic and hydrophilic states. To our knowledge, this is the first hydrogel-only artificial polymer molecular chaperone to be derived, which is also potentially a generic artificial polymer molecular chaperone for use in a folding bioreactor.