研究领域
Peptide Chemistry, Design, and Structure, Protein Folding and Design
Our lab is interested in protein structure, protein folding, and protein design. We use synthetic peptide models to study the folding problems of protein structures, including collagen, polyproline, α-helix and β-hairpin. The current research subjects include:
1.The folding and design of collagen: collagen is the most abundant protein in animals and folds into a triple helix consisting of three polyproline type II (PPII) helices. Each collagen strand is composed of approximately 300 repeats of the sequence: X-Y-Gly. Mutations of the glycine residue cause collagen abnormality and are associated with many diseases. The main work in our lab focus on the following two aspects:
•Study of the importance of glycine residues in collagen
•Design of collagen mimics for potential biomaterial
•Self-assembly of collagen-related peptides (CRPs)
2.Study of protein structures using proline derivatives
•Stereoelectronic effects on polyproline conformation: 4R-hydroxyproline (Hyp), 4S-hydroxyproline (hyp), 4R-fluoroproline (Flp), 4S-fluoroproline (flp) and other proline derivatives are used to substitute the proline (Pro) and study the stereoelectronic effects on polyproline structure.
•Investigation of how proline pucker and stereoelectronic effects affect protein stability and ligand binding affinity
3.Folding and design of small peptide models: small folding motifs including α-helices, β-hairpins, and small α/β proteins
4.Synthesis of Fmoc-protected proline derivatives for solid-phase peptide synthesis
5.Peptide-based metal sensors
•Based on small peptides, such as β-hairpins, we incorporate specific amino acids in the sequence to chelate metal ions.
•Design of peptides for the metal sensors with high selectivity and sensitivity
近期论文
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1.K. Y. Huang, C. C. Yu, and J. C. Horng*. Conjugating catalytic polyproline fragments with a self-assembling peptide produces efficient artificial hydrolases. Biomacromolecules 2020, 21, 1195-1201.
2.T. Y. Chen, W. J. Cheng, J. C. Horng, and H. Y. Hsu*. Artificial peptide-controlled protein release of Zn2+-triggered, self-assembled histidine-tagged protein microparticle. Colloids Surf. B 2020, 187, 110644.
3.K. Y. Huang and J. C. Horng*. Impacts of the terminal charged residues on polyproline conformation. J. Phys. Chem. B 2019, 123, 138-147.
4.W. H. Tseng, M. C. Li, J. C. Horng, and S. K. Wang*. Strategy and effects of polyproline peptide stapling by copper(I)-catalyzed alkyne-azide cycloaddition reaction. ChemBioChem 2019, 20, 153-158.
5.Y. H. Ting, H. J. Chen, W. J. Cheng, and J. C. Horng*. Zinc(II)-histidine induced collagen peptide assemblies: Morphology modulation and hydrolytic catalysis evaluation. Biomacromolecules 2018, 19, 2629-2637.
6.C. Y. Chen*, T. P. Ko, K. F. Lin, B. L. Lin, C. H. Huang, C. H. Chiang, J. C. Horng. NADH/NADPH bi-cofactor-utilizing and thermoactive ketol-acid reductoisomerase from Sulfolobus acidocaldarius. Sci. Rep. 2018, 8, 7176
7.P. Y. Hung, Y. H. Chen, K. Y. Huang, C. C. Yu, and J. C. Horng*. Design of polyproline-based catalysts for ester hydrolysis. ACS Omega 2017, 2, 5574-5581.
8.Y. C. Lai, C. Y. Lin, M. R. Chung, P. Y. Hung, J. C. Horng*, I. C. Chen, and L. K. Chu*. Distance-dependent excited –state electron transfer from tryptophan to gold nanoparticles through polyproline helices. J. Phys. Chem. C 2017, 121, 4882-4890.
9.C. H. Chiang, Y. H. Fu, and J. C. Horng*. Formation of AAB-type collagen heterotrimers from designed cationic and aromatic collagen-mimetic peptides: Evaluation of the C-terminal cation-p interactions. Biomacromolecules 2017, 18, 985-993.
10.P. W. Huang, J. M. Chang, and J. C. Horng*. Effects of glycosylated (2S,4R)-hydroxyproline on the stability and assembly of collagen triple helices. Amino Acids 2016, 48, 2765-2772.
11.C. H. Chiang and J. C. Horng*. Cation-p interaction induced folding of AAB-type collagen heterotrimers. J. Phys. Chem. B 2016, 120, 1205-1211.
12.Y. J. Lin, L. K. Chu, and J. C. Horng*. Effects of the terminal aromatic residues on polyproline conformation: thermodynamic and kinetic studies. J. Phys. Chem. B 2015, 119, 15796-15806.
13.K. Y. Huang and J. C. Horng*. Modulating the affinities of phosphopeptides for the human Pin1 WW domain using 4-substituted proline derivatives. Biochemistry 2015, 54, 6186-6194.
14.W. L. Hsu, T. C. Shih, and J. C. Horng*. Folding stability modulation of the villin headpiece helical subdomain by 4-fluorophenylalanine and 4-methylphenylalanine. Biopolymers 2015, 103, 627-637.
15.J. R. Hwu, M. Kapoor, R. Y. Li, Y. C. Lin, J. C. Horng, and S. C. Tsay. Synthesis of nucleobase-functionalized carbon nanotubes and their hybridization with single-stranded DNA. Chem. Asian J. 2014, 9, 3408-3412.
16.Y. J. Lin, C. H. Chang, and J. C. Horng*. The impact of 4-thiaproline on polyproline conformation. J. Phys. Chem. B 2014, 118, 10813-10820.
17.Y. J. Lin and J. C. Horng*. Impacts of terminal (4R)-fluoroproline and (4S)-fluoroproline residues on polyproline conformation. Amino Acids 2014, 46, 2317-2324.
18.H. C. Tang, Y. J. Lin, and J. C. Horng*. Modulating the folding stability and ligand binding affinity of Pin1 WW domain by proline ring puckering. Proteins 2014, 82, 67-76.
19.C. C. Hong, C. P. Chen, J. C. Horng, and S. Y. Chen. Point-of care protein sensing platform based on immuno-like membrane with molecularly-aligned nanocavities. Biosens. Bioelectron. 2013, 50, 425-430.
20.M. C. Lu, L. L. Chiu, L. Y. Chiu, C. Y. Lin, and J. C. Horng*. Highly selective and water-soluble peptidyl chemosensors for copper(II) and mercury(II) ions based on a β-hairpin structure. Anal. Methods 2013, 5, 1702-1707.
21.W. Hsu, Y. L. Chen, and J. C. Horng*. Promoting self-assembly of collagen-related peptides into various higher-order structures by metal-histidine coordination. Langmuir 2012, 28, 3194-3199.
22.Z. S. Lin, F. C. Lo, C. H. Li, C. H. Chen, W. N. Huang, I. J. Hsu, J. F. Lee, J. C. Horng, and W. F. Liaw. Peptide-bound dinitrosyliron complexes (DNICs) and neutral/reduced-form Roussin’s red esters (RREs/rRREs): understanding nitrosylation of [Fe-S] clusters leading to the formation of DNICs and RREs using a de novo design strategy. Inorg. Chem. 2011, 50, 10417-10431.
23.C. C. Chen, W. Hsu, T. C. Kao, and J. C. Horng*. Self-assembly of short collagen-related peptides into fibrils via cation-p interactions. Biochemistry 2011, 50, 2381-2383.
24.C. C. Chen, W. Hsu, K. C. Hwang, J. R. Hwu, C. C. Lin, and J. C. Horng*. Contribution of cation-p interactions to the collagen triple helix stability. Arch. Biochem. Biophys. 2011, 508, 46-53.
25.Y. S. Chen, C. C. Chen, and J. C. Horng*. Thermodynamic and kinetic consequences of substituting glycine at different positions in a Pro-Hyp-Gly repeat collagen model peptide. Biopolymers (Peptide Science) 2011, 96, 60-68.
26.T. Y. Zheng, Y. J. Lin, and J. C. Horng*. Thermodynamic consequences of incorporating 4-substituted proline derivatives into a small helical protein. Biochemistry 2010, 49, 4255-4263.
27.Y. C. Chiang, Y. J. Lin, and J. C. Horng*. Stereoelectronic effects on the transition barrier of polyproline conformational interconversion. Protein Sci. 2009, 18, 1967-1977.
28.Y. W. Chiang, T. Y. Zheng, C. J. Kao, and J. C. Horng. Determination of interspin distance distributions by CW-ESR is a single linear inverse problem. Biophys. J. 2009, 97, 930-936.
29.J. H. Cho, S. Sato, J. C. Horng, B. Anil, and D. P. Raleigh. Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Arch. Biochem. Biophys. 2008, 469, 20-28.
30.J. C. Horng, F. W. Kotch, and R. T. Raines. Is glycine a surrogate for a D-amino acid in the collagen triple helix? Protein Sci. 2007, 16, 208-215.
31.J. C. Horng, A. J. Hawk, Q. Zhao, E. S. Benedict, S. D. Burke, and R. T. Raines. Macrocyclic scaffold for the collagen triple helix. Org. Lett. 2006, 8, 4735-4738
32.Y. Li, J. C. Horng and D. P. Raleigh. pH Dependent thermodynamic and amide exchange studies of the C-terminal domain of the ribosomal protein L9: implications for unfolded state structure. Biochemistry 2006, 45, 8499-8506.
33.J. C. Horng and R. T. Raines. Stereoelectronic effects on polyproline conformation. Protein Sci. 2006, 15, 74-83
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