ridm@nrct.go.th   ระบบคลังข้อมูลงานวิจัยไทย   รายการโปรดที่คุณเลือกไว้

β-Boomerang antimicrobial and antiendotoxic peptides : lipidation and disulfide bond effects on activity and structure

หน่วยงาน Nanyang Technological University, Singapore

รายละเอียด

ชื่อเรื่อง : β-Boomerang antimicrobial and antiendotoxic peptides : lipidation and disulfide bond effects on activity and structure
นักวิจัย : Mohanram, Harini , Bhattacharjya, Surajit
คำค้น : DRNTU::Science::Medicine::Pharmacy::Pharmaceutical technology
หน่วยงาน : Nanyang Technological University, Singapore
ผู้ร่วมงาน : -
ปีพิมพ์ : 2557
อ้างอิง : Mohanram, H., & Bhattacharjya, S. (2014). β-Boomerang Antimicrobial and Antiendotoxic Peptides: Lipidation and Disulfide Bond Effects on Activity and Structure. Pharmaceuticals, 7(4), 482-501. , 1424-8247 , http://hdl.handle.net/10220/19528 , http://dx.doi.org/10.3390/ph7040482
ที่มา : -
ความเชี่ยวชาญ : -
ความสัมพันธ์ : Pharmaceuticals
ขอบเขตของเนื้อหา : -
บทคัดย่อ/คำอธิบาย :

Drug-resistant Gram-negative bacterial pathogens and endotoxin- or lipopolysaccharide (LPS)-mediated inflammations are among some of the most prominent health issues globally. Antimicrobial peptides (AMPs) are eminent molecules that can kill drug-resistant strains and neutralize LPS toxicity. LPS, the outer layer of the outer membrane of Gram-negative bacteria safeguards cell integrity against hydrophobic compounds, including antibiotics and AMPs. Apart from maintaining structural integrity, LPS, when released into the blood stream, also induces inflammatory pathways leading to septic shock. In previous works, we have reported the de novo design of a set of 12-amino acid long cationic/hydrophobic peptides for LPS binding and activity. These peptides adopt β-boomerang like conformations in complex with LPS. Structure-activity studies demonstrated some critical features of the β-boomerang scaffold that may be utilized for the further development of potent analogs. In this work, β-boomerang lipopeptides were designed and structure-activity correlation studies were carried out. These lipopeptides were homo-dimerized through a disulfide bridge to stabilize conformations and for improved activity. The designed peptides exhibited potent antibacterial activity and efficiently neutralized LPS toxicity under in vitro assays. NMR structure of C4YI13C in aqueous solution demonstrated the conserved folding of the lipopeptide with a boomerang aromatic lock stabilized with disulfide bond at the C-terminus and acylation at the N-terminus. These lipo-peptides displaying bacterial sterilization and low hemolytic activity may be useful for future applications as antimicrobial and antiendotoxin molecules.

บรรณานุกรม :
Mohanram, Harini , Bhattacharjya, Surajit . (2557). β-Boomerang antimicrobial and antiendotoxic peptides : lipidation and disulfide bond effects on activity and structure.
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Mohanram, Harini , Bhattacharjya, Surajit . 2557. "β-Boomerang antimicrobial and antiendotoxic peptides : lipidation and disulfide bond effects on activity and structure".
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Mohanram, Harini , Bhattacharjya, Surajit . "β-Boomerang antimicrobial and antiendotoxic peptides : lipidation and disulfide bond effects on activity and structure."
    กรุงเทพมหานคร : Nanyang Technological University, Singapore, 2557. Print.
Mohanram, Harini , Bhattacharjya, Surajit . β-Boomerang antimicrobial and antiendotoxic peptides : lipidation and disulfide bond effects on activity and structure. กรุงเทพมหานคร : Nanyang Technological University, Singapore; 2557.