A Naturally Occurring Peptide with an Elementary Single Disulfide-Directed β-Hairpin Fold

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Standard

A Naturally Occurring Peptide with an Elementary Single Disulfide-Directed β-Hairpin Fold. / Robinson, Samuel D; Chhabra, Sandeep; Belgi, Alessia; Chittoor, Balasubramanyam; Safavi-Hemami, Helena; Robinson, Andrea J; Papenfuss, Anthony T; Purcell, Anthony W; Norton, Raymond S.

I: Structure, Bind 24, Nr. 2, 2016, s. 293-299.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Robinson, SD, Chhabra, S, Belgi, A, Chittoor, B, Safavi-Hemami, H, Robinson, AJ, Papenfuss, AT, Purcell, AW & Norton, RS 2016, 'A Naturally Occurring Peptide with an Elementary Single Disulfide-Directed β-Hairpin Fold', Structure, bind 24, nr. 2, s. 293-299. https://doi.org/10.1016/j.str.2015.11.015

APA

Robinson, S. D., Chhabra, S., Belgi, A., Chittoor, B., Safavi-Hemami, H., Robinson, A. J., Papenfuss, A. T., Purcell, A. W., & Norton, R. S. (2016). A Naturally Occurring Peptide with an Elementary Single Disulfide-Directed β-Hairpin Fold. Structure, 24(2), 293-299. https://doi.org/10.1016/j.str.2015.11.015

Vancouver

Robinson SD, Chhabra S, Belgi A, Chittoor B, Safavi-Hemami H, Robinson AJ o.a. A Naturally Occurring Peptide with an Elementary Single Disulfide-Directed β-Hairpin Fold. Structure. 2016;24(2):293-299. https://doi.org/10.1016/j.str.2015.11.015

Author

Robinson, Samuel D ; Chhabra, Sandeep ; Belgi, Alessia ; Chittoor, Balasubramanyam ; Safavi-Hemami, Helena ; Robinson, Andrea J ; Papenfuss, Anthony T ; Purcell, Anthony W ; Norton, Raymond S. / A Naturally Occurring Peptide with an Elementary Single Disulfide-Directed β-Hairpin Fold. I: Structure. 2016 ; Bind 24, Nr. 2. s. 293-299.

Bibtex

@article{d79f81d0b06845839c51184b08631071,

title = "A Naturally Occurring Peptide with an Elementary Single Disulfide-Directed β-Hairpin Fold",

abstract = "Certain peptide folds, owing to a combination of intrinsic stability and resilience to amino acid substitutions, are particularly effective for the display of diverse functional groups. Such {"}privileged scaffolds{"} are valuable as starting points for the engineering of new bioactive molecules. We have identified a precursor peptide expressed in the venom gland of the marine snail Conus victoriae, which appears to belong to a hitherto undescribed class of molluscan neuropeptides. Mass spectrometry matching with the venom confirmed the complete mature peptide sequence as a 31-residue peptide with a single disulfide bond. Solution structure determination revealed a unique peptide fold that we have designated the single disulfide-directed β hairpin (SDH). The SDH fold is highly resistant to thermal denaturation and forms the core of several other multiple disulfide-containing peptide folds, including the inhibitor cystine knot. This elementary fold may offer a valuable starting point for the design and engineering of new bioactive peptides. ",

keywords = "Animals, Cysteine, Mass Spectrometry, Models, Molecular, Mollusk Venoms/chemistry, Neuropeptides/chemistry, Peptides/chemistry, Protein Folding, Protein Structure, Secondary, Snails/chemistry",

author = "Robinson, {Samuel D} and Sandeep Chhabra and Alessia Belgi and Balasubramanyam Chittoor and Helena Safavi-Hemami and Robinson, {Andrea J} and Papenfuss, {Anthony T} and Purcell, {Anthony W} and Norton, {Raymond S}",

year = "2016",

doi = "10.1016/j.str.2015.11.015",

language = "English",

volume = "24",

pages = "293--299",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "2",

}

RIS

TY - JOUR

T1 - A Naturally Occurring Peptide with an Elementary Single Disulfide-Directed β-Hairpin Fold

AU - Robinson, Samuel D

AU - Chhabra, Sandeep

AU - Belgi, Alessia

AU - Chittoor, Balasubramanyam

AU - Safavi-Hemami, Helena

AU - Robinson, Andrea J

AU - Papenfuss, Anthony T

AU - Purcell, Anthony W

AU - Norton, Raymond S

PY - 2016

Y1 - 2016

N2 - Certain peptide folds, owing to a combination of intrinsic stability and resilience to amino acid substitutions, are particularly effective for the display of diverse functional groups. Such "privileged scaffolds" are valuable as starting points for the engineering of new bioactive molecules. We have identified a precursor peptide expressed in the venom gland of the marine snail Conus victoriae, which appears to belong to a hitherto undescribed class of molluscan neuropeptides. Mass spectrometry matching with the venom confirmed the complete mature peptide sequence as a 31-residue peptide with a single disulfide bond. Solution structure determination revealed a unique peptide fold that we have designated the single disulfide-directed β hairpin (SDH). The SDH fold is highly resistant to thermal denaturation and forms the core of several other multiple disulfide-containing peptide folds, including the inhibitor cystine knot. This elementary fold may offer a valuable starting point for the design and engineering of new bioactive peptides.

AB - Certain peptide folds, owing to a combination of intrinsic stability and resilience to amino acid substitutions, are particularly effective for the display of diverse functional groups. Such "privileged scaffolds" are valuable as starting points for the engineering of new bioactive molecules. We have identified a precursor peptide expressed in the venom gland of the marine snail Conus victoriae, which appears to belong to a hitherto undescribed class of molluscan neuropeptides. Mass spectrometry matching with the venom confirmed the complete mature peptide sequence as a 31-residue peptide with a single disulfide bond. Solution structure determination revealed a unique peptide fold that we have designated the single disulfide-directed β hairpin (SDH). The SDH fold is highly resistant to thermal denaturation and forms the core of several other multiple disulfide-containing peptide folds, including the inhibitor cystine knot. This elementary fold may offer a valuable starting point for the design and engineering of new bioactive peptides.

KW - Animals

KW - Cysteine

KW - Mass Spectrometry

KW - Models, Molecular

KW - Mollusk Venoms/chemistry

KW - Neuropeptides/chemistry

KW - Peptides/chemistry

KW - Protein Folding

KW - Protein Structure, Secondary

KW - Snails/chemistry

U2 - 10.1016/j.str.2015.11.015

DO - 10.1016/j.str.2015.11.015

M3 - Journal article

C2 - 26774129

VL - 24

SP - 293

EP - 299

JO - Structure

JF - Structure

SN - 0969-2126

IS - 2

ER -

ID: 232824113