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- ISSN: 0929-8665
- E-ISSN: 1875-5305
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Conformational Stability and Activity of Circular Enterocin AS-48 Derivatives
- Source: Protein and Peptide Letters, Volume 17, Issue 6, Jun 2010, p. 708 - 714
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- 01 Jun 2010
Abstract
Four AS-48 mutants (Trp24Ala, Gly13Lys, Leu40Lys and Ala53Ser) were obtained by site-directed mutagenesis. The minimal inhibitory concentration of each peptide showed that only residue Trp24 was unquestionably involved in the biological activity. Guanidine hydrochloride-induced unfolding assays showed a three-state transition denaturation process, suggesting a molten-globule-like conformation after the first transition.
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