Applications and evolution of melittin, the quintessential membrane active peptide

Shantanu Guha; Ryan P. Ferrie; Jenisha Ghimire; Cristina R. Ventura; Eric Wu; Leisheng Sun; Sarah Y. Kim; Gregory R. Wiedman; Kalina Hristova; Wimley C. Wimley

doi:10.1016/j.bcp.2021.114769

Applications and evolution of melittin, the quintessential membrane active peptide

Shantanu Guha, Ryan P. Ferrie, Jenisha Ghimire, Cristina R. Ventura, Eric Wu, Leisheng Sun, Sarah Y. Kim, Gregory R. Wiedman, Kalina Hristova, Wimley C. Wimley

Research output: Contribution to journal › Review article › peer-review

Abstract

Melittin, the main venom component of the European Honeybee, is a cationic linear peptide-amide of 26 amino acid residues with the sequence: GIGAVLKVLTTGLPALISWIKRKRQQ-NH₂. Melittin binds to lipid bilayer membranes, folds into amphipathic α-helical secondary structure and disrupts the permeability barrier. Since melittin was first described, a remarkable array of activities and potential applications in biology and medicine have been described. Melittin is also a favorite model system for biophysicists to study the structure, folding and function of peptides and proteins in membranes. Melittin has also been used as a template for the evolution of new activities in membranes. Here we overview the rich history of scientific research into the many activities of melittin and outline exciting future applications.

Original language	English (US)
Article number	114769
Journal	Biochemical Pharmacology
Volume	193
DOIs	https://doi.org/10.1016/j.bcp.2021.114769
State	Published - Nov 2021
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Pharmacology

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10.1016/j.bcp.2021.114769

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title = "Applications and evolution of melittin, the quintessential membrane active peptide",

abstract = "Melittin, the main venom component of the European Honeybee, is a cationic linear peptide-amide of 26 amino acid residues with the sequence: GIGAVLKVLTTGLPALISWIKRKRQQ-NH2. Melittin binds to lipid bilayer membranes, folds into amphipathic α-helical secondary structure and disrupts the permeability barrier. Since melittin was first described, a remarkable array of activities and potential applications in biology and medicine have been described. Melittin is also a favorite model system for biophysicists to study the structure, folding and function of peptides and proteins in membranes. Melittin has also been used as a template for the evolution of new activities in membranes. Here we overview the rich history of scientific research into the many activities of melittin and outline exciting future applications.",

author = "Shantanu Guha and Ferrie, {Ryan P.} and Jenisha Ghimire and Ventura, {Cristina R.} and Eric Wu and Leisheng Sun and Kim, {Sarah Y.} and Wiedman, {Gregory R.} and Kalina Hristova and Wimley, {Wimley C.}",

note = "Publisher Copyright: {\textcopyright} 2021",

year = "2021",

month = nov,

doi = "10.1016/j.bcp.2021.114769",

language = "English (US)",

volume = "193",

journal = "Biochemical Pharmacology",

issn = "0006-2952",

publisher = "Elsevier Inc.",

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T1 - Applications and evolution of melittin, the quintessential membrane active peptide

AU - Guha, Shantanu

AU - Ferrie, Ryan P.

AU - Ghimire, Jenisha

AU - Ventura, Cristina R.

AU - Wu, Eric

AU - Sun, Leisheng

AU - Kim, Sarah Y.

AU - Wiedman, Gregory R.

AU - Hristova, Kalina

AU - Wimley, Wimley C.

PY - 2021/11

Y1 - 2021/11

N2 - Melittin, the main venom component of the European Honeybee, is a cationic linear peptide-amide of 26 amino acid residues with the sequence: GIGAVLKVLTTGLPALISWIKRKRQQ-NH2. Melittin binds to lipid bilayer membranes, folds into amphipathic α-helical secondary structure and disrupts the permeability barrier. Since melittin was first described, a remarkable array of activities and potential applications in biology and medicine have been described. Melittin is also a favorite model system for biophysicists to study the structure, folding and function of peptides and proteins in membranes. Melittin has also been used as a template for the evolution of new activities in membranes. Here we overview the rich history of scientific research into the many activities of melittin and outline exciting future applications.

AB - Melittin, the main venom component of the European Honeybee, is a cationic linear peptide-amide of 26 amino acid residues with the sequence: GIGAVLKVLTTGLPALISWIKRKRQQ-NH2. Melittin binds to lipid bilayer membranes, folds into amphipathic α-helical secondary structure and disrupts the permeability barrier. Since melittin was first described, a remarkable array of activities and potential applications in biology and medicine have been described. Melittin is also a favorite model system for biophysicists to study the structure, folding and function of peptides and proteins in membranes. Melittin has also been used as a template for the evolution of new activities in membranes. Here we overview the rich history of scientific research into the many activities of melittin and outline exciting future applications.

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DO - 10.1016/j.bcp.2021.114769

M3 - Review article

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SN - 0006-2952

VL - 193

JO - Biochemical Pharmacology

JF - Biochemical Pharmacology

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ER -

Applications and evolution of melittin, the quintessential membrane active peptide

Abstract

ASJC Scopus subject areas

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