Solution structure of an antimicrobial peptide buforin II

Yi, Gwan‐Su; Park, Chan Bae; Kim, Sun Chang; Cheong, Chaejoon

doi:10.1016/s0014-5793(96)01193-3

Cited by 80 publications

(68 citation statements)

References 22 publications

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“…However, the distorted helical conformation of buforin II (residues 5-13) caused by proline may be related to efficient translocation. Buforin II conforms to a bent helix with the flexible N-terminal region in trifluoroethanol͞buffer and probably in lipid bilayer (14). The unusual helical conformation of the proline-hinge region (residues 5-13) may provide a flexibility that is related to efficient translocation via an unknown mechanism caused by the distorted helical conformation with a larger diameter and a larger pitch.…”

Section: Discussionmentioning

confidence: 99%

“…Designed synthetic buforin II analogs consisting of five repeats of the C-terminal regular ␣-helical motif RLLR or three repeats of RVHRLLR were also synthesized to evaluate the importance of the C-terminal amphipathic helix. In addition, to study the role of the extended ␣-helical region BUF (5-13) containing a proline hinge, we synthesized two hybrid peptides, BUF (5)(6)(7)(8)(9)(10)(11)(12)(13)[RLLR] 3 and BUF (5-13)MG (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14). BUF (5)(6)(7)(8)(9)(10)(11)(12)(13)[RLLR] 3 contained BUF (5-13) and three repeats of the regular ␣-helical motif RLLR.…”

Section: Methodsmentioning

confidence: 99%

“…BUF (5)(6)(7)(8)(9)(10)(11)(12)(13)[RLLR] 3 contained BUF (5-13) and three repeats of the regular ␣-helical motif RLLR. BUF (5-13)MG (1-14) consisted of BUF (5)(6)(7)(8)(9)(10)(11)(12)(13) and the N-terminal ␣-helix [MG (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)] of magainin II.…”

Section: Methodsmentioning

confidence: 99%

“…Buforin II has a helix-hinge-helix structure; the N-terminal extended helix includes residues 5 to 10, and the C-terminal helix includes residues 12 to 21. The helices are separated by a proline residue situated at amino acid position 11 (14). This two-helix organization and unique mode of action make buforin II a highly attractive candidate for deciphering the role of each structural element in conferring on buforin II its highly potent antimicrobial activity.…”

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confidence: 99%

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Structure–activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II

Park

Yi²,

Matsuzaki³

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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Buforin II is a 21-aa potent antimicrobial peptide that forms, in a hydrophobic medium, an amphipathic structure consisting of an N-terminal random coil region (residues 1-4), an extended helical region (residues 5-10), a hinge (residue 11), and a C-terminal regular ␣-helical region (residues 12-21). To elucidate the structural features of buforin II that are required for its potent antimicrobial activity, we synthesized a series of N-and C-terminally truncated or amino acid-substituted synthetic buforin II analogs and examined their antimicrobial activity and mechanism of action. Deletion of the N-terminal random coil region increased the antibacterial activity Ϸ2-fold, but further N-terminal truncation yielded peptide analogs with progressively decreasing activity. Removal of four amino acids from the C-terminal end of buforin II resulted in a complete loss of antimicrobial activity. The substitution of leucine for the proline hinge decreased significantly the antimicrobial activity. Confocal fluorescence microscopic studies showed that buforin II analogs with a proline hinge penetrated the cell membrane without permeabilization and accumulated in the cytoplasm. However, removal of the proline hinge abrogated the ability of the peptide to enter cells, and buforin II analogs without a proline hinge localized on the cell surface, permeabilizing the cell membrane. In addition, the cell-penetrating efficiency of buforin II and its truncated analogs, which depended on the ␣-helical content of the peptides, correlated linearly with their antimicrobial potency. Our results demonstrate clearly that the proline hinge is responsible for the cell-penetrating ability of buforin II, and the cellpenetrating efficiency determines the antimicrobial potency of the peptide.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Structure–activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II

Park

Yi²,

Matsuzaki³

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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479

385

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“…The inner diameter is approximately 3.0-5.0 nm and the external diameter is approximately 7.0-8.4 nm. Each channel is formed by approximately 4-7 magainins and 90 lipid molecules (122)(123)(124). iv.…”

Section: Mechanism Of Actionmentioning

confidence: 99%

Antimicrobial peptides from amphibians

Xiao

Liu

Lai

2011

BioMolecular Concepts

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Increased prevalence of multi-drug resistance in pathogens has encouraged researchers to focus on finding novel forms of anti-infective agents. Antimicrobial peptides (AMPs) found in animal secretions are components of host innate immune response and have survived eons of pathogen evolution. Thus, they are likely to be active against pathogens and even those that are resistant to conventional drugs. Many peptides have been isolated and shown to be effective against multi-drug resistant pathogens. More than 500 AMPs have been identified from amphibians. The abundance of AMPs in frog skin is remarkable and constitutes a rich source for design of novel pharmaceutical molecules. Expression and post-translational modifications, discovery, activities and probable therapeutic application prospects of amphibian AMPs will be discussed in this article.

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