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Evaluation of orientation-dependent cation−π pairwise effects within collagen triple helices: the lateral, N-to-C axial, and C-to-N axial cation−π pairs have distinct effects on the collagen triple helix. The contribution of individual pairs can be used to predict the stability of a homotrimer.
Published in J. Phys. Chem. B 2025
https://pubs.acs.org/doi/10.1021/acs.jpcb.4c08691
PMCID# PMC12086834
Also refer to the highlight: https://archive.benchmarkemail.com/beer_beer/newsletter/國科會自然處《化學圖書服務計畫》114年7月號電子報
Consequences of incorporating thiaproline and its oxidized derivatives into collagen triple helices: Thiaproline (Thp) was shown to slightly affect the collagen triple helix at X-position but significantly destabilize the trimer at Y-position. In particular, the oxidized derivative, S,S-dioxide Thp at Y-position would make CMPs fail to fold into trimers.
Published in Protein Sci. 2023
https://doi.org/10.1002/pro.4650
Modulating the collagen triple helix stability by terminal charged residues: the cationic residues (Lys, ornithine) or the anionic residues (Glu, Asp) were incorporated into the peptide termini to study the effects on the triple helix stability.
Published in J. Phys. Chem. B 2021
Design of efficient hydrolases by conjugating oligoproline and self-assembling peptides
Design of efficient hydrolases by conjugating oligoproline and self-assembling peptides
Published in Biomacromolecules 2020
Using polyproline II structure as a scaffold to design peptide-based hydrolases
Using polyproline II structure as a scaffold to design peptide-based hydrolases
Published in ACS Omega 2017
Zn(II) ions induce collagen-mimetic peptides to assemble into various morphological high-order structures, and the assemblies exhibit catalytic activity on ester hydrolysis.
Zn(II) ions induce collagen-mimetic peptides to assemble into various morphological high-order structures, and the assemblies exhibit catalytic activity on ester hydrolysis.
Published in Biomacromolecules 2018
The designed collagen-mimetic peptides were induced by various metal ion to proceed self-assembly and form higher-order structures. The assembled fibrils exhibit a D-period pattern and the size of assemblies is correlated with the assembly rate.
Published in Langmuir 2011
Cation-π interactions were applied to assemble short collagen-mimetic peptides into fibrils.
Published in Biochemistry 2011
Cation-π interactions can successfully induce the folding of collagen heterotrimers.
Published in J. Phys. Chem. B 2016
The C-terminal cation-π interactions can further control the composition of collagen heterotrimers.
Published in Biomacromolecules 2017
Effects of the terminal charged residues on polyproline confromation: the incorporation of cationic residues (Arg, Lys) into the C-terminus stabilizes the PPII structure and prohibit its conversion to the PPI structure.
Published in J. Phys. Chem. B 2019
Effects of the terminal aromatic residues on polyproline confromation: the incorporation of aromatic residues (Phe, Tyr, Trp) into either the C- or N-terminus favors the formation of PPI structure.
Published in J. Phys. Chem. B 2015
Fluorophenylalanine and methylphenylalanine could modulate the interactions in the hydrophbic core of protein HP36.
Published in Biopolymers 2015
4-Substituted proline derivatives were used to design the peptide inhibitor for the WW domain. (2S,4R)-fluoroproline incorporated peptide exhibits the best affinity to the WW domain.
Published in Biochemistry 2015
Modulating the stability and ligand affinity of a β-protein (the WW domain) by 4-substituted proline derivatives.
Published in Proteins 2014
Modulating the stability of a α-helical protein (HP36) by 4-substituted proline derivatives.
Published in Biochemistry 2010
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