Self-Assembly of Lipopeptides Containing Short Peptide Fragments Derived from the Gastrointestinal Hormone PYY3-36: From Micelles to Amyloid Fibrils

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Self-Assembly of Lipopeptides Containing Short Peptide Fragments Derived from the Gastrointestinal Hormone PYY3-36 : From Micelles to Amyloid Fibrils. / Hutchinson, Jessica A.; Hamley, Ian W.; Torras, Juan; Alemán, Carlos; Seitsonen, Jani; Ruokolainen, Janne.

In: Journal of Physical Chemistry B, Vol. 123, No. 3, 24.01.2019, p. 614-621.

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@article{87dc493a362045f19d734c298bf7da4a,
title = "Self-Assembly of Lipopeptides Containing Short Peptide Fragments Derived from the Gastrointestinal Hormone PYY3-36: From Micelles to Amyloid Fibrils",
abstract = "We investigate the impact of lipidation on the self-assembly of two peptide fragments from the gastrointestinal peptide hormone PYY3-36. The lipopeptides C16IKPEAP and C16IKPEAPGE contain the first 6 and 8 amino acid residues, respectively, from the PYY3-36 peptide sequence, with a palmitoyl C16 tail attached at the N-terminus. These lipopeptides form spherical micelles in aqueous solution, above a critical micelle concentration (cmc), which is pH-dependent. Modeling of small-angle X-ray scattering data along with molecular dynamics simulations shows the formation of micelles with a hydrophobic interior and a well-hydrated exterior. The lipopeptides have a disordered conformation over the pH and temperature ranges studied. The cmc is found to be independent of temperature, pointing to athermal micellization. In contrast to the presence of hydrated micelles in solution, β-sheet amyloid fibrils form in dried samples. Thus, the nanostructure of lipidated PYY3-36 fragment peptides can be tuned by control of pH or concentration, for future applications.",
author = "Hutchinson, {Jessica A.} and Hamley, {Ian W.} and Juan Torras and Carlos Alem{\'a}n and Jani Seitsonen and Janne Ruokolainen",
year = "2019",
month = "1",
day = "24",
doi = "10.1021/acs.jpcb.8b11097",
language = "English",
volume = "123",
pages = "614--621",
journal = "Journal of Physical Chemistry B",
issn = "1520-6106",
publisher = "AMERICAN CHEMICAL SOCIETY",
number = "3",

}

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TY - JOUR

T1 - Self-Assembly of Lipopeptides Containing Short Peptide Fragments Derived from the Gastrointestinal Hormone PYY3-36

T2 - From Micelles to Amyloid Fibrils

AU - Hutchinson, Jessica A.

AU - Hamley, Ian W.

AU - Torras, Juan

AU - Alemán, Carlos

AU - Seitsonen, Jani

AU - Ruokolainen, Janne

PY - 2019/1/24

Y1 - 2019/1/24

N2 - We investigate the impact of lipidation on the self-assembly of two peptide fragments from the gastrointestinal peptide hormone PYY3-36. The lipopeptides C16IKPEAP and C16IKPEAPGE contain the first 6 and 8 amino acid residues, respectively, from the PYY3-36 peptide sequence, with a palmitoyl C16 tail attached at the N-terminus. These lipopeptides form spherical micelles in aqueous solution, above a critical micelle concentration (cmc), which is pH-dependent. Modeling of small-angle X-ray scattering data along with molecular dynamics simulations shows the formation of micelles with a hydrophobic interior and a well-hydrated exterior. The lipopeptides have a disordered conformation over the pH and temperature ranges studied. The cmc is found to be independent of temperature, pointing to athermal micellization. In contrast to the presence of hydrated micelles in solution, β-sheet amyloid fibrils form in dried samples. Thus, the nanostructure of lipidated PYY3-36 fragment peptides can be tuned by control of pH or concentration, for future applications.

AB - We investigate the impact of lipidation on the self-assembly of two peptide fragments from the gastrointestinal peptide hormone PYY3-36. The lipopeptides C16IKPEAP and C16IKPEAPGE contain the first 6 and 8 amino acid residues, respectively, from the PYY3-36 peptide sequence, with a palmitoyl C16 tail attached at the N-terminus. These lipopeptides form spherical micelles in aqueous solution, above a critical micelle concentration (cmc), which is pH-dependent. Modeling of small-angle X-ray scattering data along with molecular dynamics simulations shows the formation of micelles with a hydrophobic interior and a well-hydrated exterior. The lipopeptides have a disordered conformation over the pH and temperature ranges studied. The cmc is found to be independent of temperature, pointing to athermal micellization. In contrast to the presence of hydrated micelles in solution, β-sheet amyloid fibrils form in dried samples. Thus, the nanostructure of lipidated PYY3-36 fragment peptides can be tuned by control of pH or concentration, for future applications.

UR - http://www.scopus.com/inward/record.url?scp=85060313089&partnerID=8YFLogxK

U2 - 10.1021/acs.jpcb.8b11097

DO - 10.1021/acs.jpcb.8b11097

M3 - Article

VL - 123

SP - 614

EP - 621

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

SN - 1520-6106

IS - 3

ER -

ID: 31643586