Synthetic peptide and template-assembled synthetic protein models of the hen egg white lysozyme 87–97 helix: Importance of a protein-like framework for conformational stability in a short peptide sequence
✍ Scribed by Stéphane Vuilleumier; Manfred Mutter
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1993
- Tongue
- English
- Weight
- 1008 KB
- Volume
- 33
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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 [