| Literature DB >> 26782986 |
Estelle Yaba Adje1, Rafik Balti2, Didier Lecouturier1, Mostafa Kouach3, Pascal Dhulster1, Didier Guillochon1, Naïma Nedjar-Arroume1.
Abstract
The use of antimicrobial peptides (AMPs) is an alternative to traditional antibiotics. AMPs are obtained using different methods such as bacterial synthesis, chemical synthesis and controlled enzymatic hydrolysis. The later is an interesting approach that deserves our attention because of the yields gathered and peptides engineered. Usually, activities of AMPs obtained in such a way are tightly dependent on the hydrolysis mechanism used. This paper deals with the hydrolysis of hemoglobin mechanism as a potential source of AMPs. Production of AMPs from hemoglobin using enzymatic controlled system is linked to hemoglobin structure. Further, we show that bovine hemoglobin, which is sensitive to peptic hydrolysis, results upon enzymatic digestion as a great source of AMPs. The hemoglobin in native and denatured states was hydrolyzed by "one-by-one" and "zipper" mechanisms, respectively. Nevertheless, a new mechanism named "semi-zipper" mechanism is obtained when protein is in molten globule structural state, constituting an original strategy for AMPs production. Seventy seven percentage of the peptides obtained by this new strategy showed antibacterial activity against nine strains.Entities:
Keywords: Antimicrobial peptides; Bovine hemoglobin; Hydrolysis mechanism; Protein structure
Year: 2013 PMID: 26782986 DOI: 10.1007/s12602-013-9138-y
Source DB: PubMed Journal: Probiotics Antimicrob Proteins ISSN: 1867-1306 Impact factor: 4.609