Different Effects of 4-Hydroxyproline and 4-Fluoroproline on the Stability of Collagen Triple Helix

Differential scanning calorimetry (DSC) analyses of a series of collagen model peptides suggest that 4-hydroxyproline (Hyp) and 4-fluoroproline (fPro) have different effects on the stability of the collagen triple helices according to the sequence of amino acids and stereochemistry at the 4 position...

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Bibliographic Details
Published in:Biochemistry (Easton) 2005-04, Vol.44 (16), p.6034-6042
Main Authors: Nishi, Yoshinori, Uchiyama, Susumu, Doi, Masamitsu, Nishiuchi, Yuji, Nakazawa, Takashi, Ohkubo, Tadayasu, Kobayashi, Yuji
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Calorimetry, Differential Scanning
Circular Dichroism
Collagen - chemistry
Drug Stability
Hydroxyproline - chemistry
In Vitro Techniques
Molecular Weight
Nuclear Magnetic Resonance, Biomolecular
Peptides - chemical synthesis
Peptides - chemistry
Proline - analogs & derivatives
Proline - chemistry
Protein Structure, Secondary
Thermodynamics
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Summary:Differential scanning calorimetry (DSC) analyses of a series of collagen model peptides suggest that 4-hydroxyproline (Hyp) and 4-fluoroproline (fPro) have different effects on the stability of the collagen triple helices according to the sequence of amino acids and stereochemistry at the 4 positions of these imino acids. The thermodynamic parameters indicate that the enhanced stabilities are classified into two different types:  the enthalpy term is primarily responsible for the enhanced stability of the triple helix of (Pro-Hyp R -Gly)10, whereas the entropy term dominates the enhanced stability of (Pro-fPro R -Gly)10. The difference between the molecular volumes observed in solution and intrinsic molecular volumes calculated from the crystal structure indicates the different hydration states of these peptides. (Pro-Hyp R -Gly)10 is highly hydrated compared to (Pro-Pro-Gly)10, which contributes to the larger enthalpy. In contrast, the volume of (Pro-fPro R -Gly)10 shows a smaller degree of hydration than that of (Pro-Pro-Gly)10. The entropic cost of forming the triple helix of the fPro-containing peptides is compensated by a decrease in an ordered structure of water molecules surrounding the peptide molecule, although the contribution of enthalpy originating from the hydration is reduced. These arguments about the different contribution of entropic and enthalpic terms were successfully applied to interpret the stability of the triple helix of (fPro S -Pro-Gly)10 as well.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi047887m