Investigating the role of (2S,4R)-4-hydroxyproline in elastin model peptides
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Investigating the role of (2S,4R)-4-hydroxyproline in elastin model peptides. / Bochicchio, Brigida; Laurita, Alessandro; Heinz, Andrea; Schmelzer, Christian E H; Pepe, Antonietta.
In: Biomacromolecules, Vol. 14, No. 12, 09.12.2013, p. 4278-88.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Investigating the role of (2S,4R)-4-hydroxyproline in elastin model peptides
AU - Bochicchio, Brigida
AU - Laurita, Alessandro
AU - Heinz, Andrea
AU - Schmelzer, Christian E H
AU - Pepe, Antonietta
PY - 2013/12/9
Y1 - 2013/12/9
N2 - Post-translational modifications play a key role in defining the biological functions of proteins. Among them, the hydroxylation of proline producing the (2S,4R)-4-hydroxyproline (Hyp) is one of the most frequent modifications observed in vertebrates, being particularly abundant in the proteins of the extracellular matrix. In collagen, hydroxylation of proline plays a critical role, conferring the correct structure and mechanical strength to collagen fibers. In elastin, the exact role of this modification is not yet understood. Here we show that Hyp-containing elastin polypeptides have flexible molecular structures, analogously to proline-containing polypeptides. In turn, the self-assembly of the elastin peptides is significantly altered by the presence of Hyp, evidencing different supramolecular structures. Also the in vitro susceptibility to protease digestion is changed. These findings give a better insight into the elastic fiber formation and degradation processes in the extracellular matrix. Furthermore, our results could contribute in defining the subtle role of proline structural variants in the folding and self-assembly of elastin-inspired peptides, helping the rational design of elastin biomaterials.
AB - Post-translational modifications play a key role in defining the biological functions of proteins. Among them, the hydroxylation of proline producing the (2S,4R)-4-hydroxyproline (Hyp) is one of the most frequent modifications observed in vertebrates, being particularly abundant in the proteins of the extracellular matrix. In collagen, hydroxylation of proline plays a critical role, conferring the correct structure and mechanical strength to collagen fibers. In elastin, the exact role of this modification is not yet understood. Here we show that Hyp-containing elastin polypeptides have flexible molecular structures, analogously to proline-containing polypeptides. In turn, the self-assembly of the elastin peptides is significantly altered by the presence of Hyp, evidencing different supramolecular structures. Also the in vitro susceptibility to protease digestion is changed. These findings give a better insight into the elastic fiber formation and degradation processes in the extracellular matrix. Furthermore, our results could contribute in defining the subtle role of proline structural variants in the folding and self-assembly of elastin-inspired peptides, helping the rational design of elastin biomaterials.
KW - Amino Acid Sequence
KW - Animals
KW - Circular Dichroism
KW - Humans
KW - Hydroxylation
KW - Hydroxyproline
KW - Magnetic Resonance Spectroscopy
KW - Microscopy, Atomic Force
KW - Microscopy, Electron, Transmission
KW - Molecular Sequence Data
KW - Nanofibers
KW - Peptide Fragments
KW - Protein Processing, Post-Translational
KW - Protein Structure, Secondary
KW - Tropoelastin
KW - Journal Article
KW - Research Support, Non-U.S. Gov't
U2 - 10.1021/bm4011529
DO - 10.1021/bm4011529
M3 - Journal article
C2 - 24127724
VL - 14
SP - 4278
EP - 4288
JO - Biomacromolecules
JF - Biomacromolecules
SN - 1525-7797
IS - 12
ER -
ID: 186422042