Abstract:
:In the native structure of hen egg white lysozyme (HEL), the amino acid sequence 87-97 (HEL 87-97) forms an amphiphilic helix, with hydrophilic residues in the sequence directed toward the solvent. A synthetic version of the HEL 87-97 sequence (with the cysteine corresponding to position 94 of HEL replaced by alanine) displays conformational features in solution typical of an unordered structure as judged by CD. However, various modifications in the sequence result in increased helix-forming potential of the HEL 87-97 analogues. Further stabilization of the helical conformation in the most helical analogue of the HEL 87-97 sequence is obtained when 4 copies of this peptide sequence are coupled on a peptide carrier molecule following the template-assembled synthetic protein (TASP) approach [M. Mutter and S. Vuilleumier (1989) Angew. Chem. Int. Ed. Engl., Vol. 28, pp. 535-554 "A Chemical Approach to Protein Design-Template-Assembled Synthetic Proteins (TASP)." This suggests that long-range interactions of the peptide with its environment contribute to conformational stability in short peptide sequences. TASP molecules may prove useful for the study of the factors that determine secondary structure formation in short peptides by providing a protein-like framework.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Vuilleumier S,Mutter Mdoi
10.1002/bip.360330307subject
Has Abstractpub_date
1993-03-01 00:00:00pages
389-400issue
3eissn
0006-3525issn
1097-0282journal_volume
33pub_type
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