Conformational stability and activity of circular Enterocin AS-48 derivatives.
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.
Sánchez-Hidalgo
Marina
M
Department de Microbiología, Facultad de Ciencias, Universidad de Granada, Spain.
Fernández-Escamilla
Ana M
AM
Martínez-Bueno
Manuel
M
Valdivia
Eva
E
Serrano
Luis
L
Maqueda
Mercedes
M
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
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D010455:Peptides; C051034:BacA protein, Enterococcus faecalis; D014364:Tryptophan; D019791:Guanidine