Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins
被引:101
作者:
Wang, Guangshun
论文数: 0引用数: 0
h-index: 0
机构:
Univ Nebraska Med Ctr, Eppley Inst Res Canc & Allied Dis, Struct Fun Lab, Omaha, NE 68198 USAUniv Nebraska Med Ctr, Eppley Inst Res Canc & Allied Dis, Struct Fun Lab, Omaha, NE 68198 USA
Wang, Guangshun
[1
]
Watson, Karen M.
论文数: 0引用数: 0
h-index: 0
机构:
ImQuest BioSci Inc, Frederick, MD 21704 USAUniv Nebraska Med Ctr, Eppley Inst Res Canc & Allied Dis, Struct Fun Lab, Omaha, NE 68198 USA
Watson, Karen M.
[2
]
Buckheit, Robert W., Jr.
论文数: 0引用数: 0
h-index: 0
机构:
ImQuest BioSci Inc, Frederick, MD 21704 USAUniv Nebraska Med Ctr, Eppley Inst Res Canc & Allied Dis, Struct Fun Lab, Omaha, NE 68198 USA
Buckheit, Robert W., Jr.
[2
]
机构:
[1] Univ Nebraska Med Ctr, Eppley Inst Res Canc & Allied Dis, Struct Fun Lab, Omaha, NE 68198 USA
From among 15 human cathelicidin LL-37-derived peptides, FK-13 was identified as the smallest peptide active against human immunodeficiency virus (HIV) and GI-20 had the highest therapeutic index, which was twice that of LL-37. BMAP-18, which is derived from bovine cathelicidin BMAP-27, possessed a therapeutic index similar to that of GI-20. Peptide sequence order, helical structures, and aromatic residues are important in HIV inhibition.