title: Conformational stability and activity of circular Enterocin AS-48 derivatives.
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.
authors: Department de Microbiología, Facultad de Ciencias, Universidad de Granada, Spain.
authors: Marina
authors: M
authors: Sánchez-Hidalgo
authors: Ana M
authors: AM
authors: Fernández-Escamilla
authors: Manuel
authors: M
authors: Martínez-Bueno
authors: Eva
authors: E
authors: Valdivia
authors: Luis
authors: L
authors: Serrano
authors: Mercedes
authors: M
authors: Maqueda
mesh_terms: D000465:Algorithms; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000494:pharmacology; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000494:pharmacology; D002942:Circular Dichroism; D013293:Enterococcus faecalis / Q000737:chemistry* / Q000235:genetics; D019791:Guanidine / Q000737:chemistry / Q000494:pharmacology; D007700:Kinetics; D008826:Microbial Sensitivity Tests; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000494:pharmacology; D011487:Protein Conformation; D017510:Protein Folding / Q000187:drug effects; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D013696:Temperature; D013816:Thermodynamics; D014364:Tryptophan / Q000737:chemistry / Q000235:genetics
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D010455:Peptides; C051034:BacA protein, Enterococcus faecalis; D014364:Tryptophan; D019791:Guanidine