Welcome to JCH Lab (洪嘉呈實驗室）

A Laboratory Devoted to Protein/Peptide Chemistry, Folding, Assembly, and Design

Research Interests

Our lab is mainly interested in protein/peptide structure, folding, and 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 assembly of collagen-mimetic peptides: 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. 

• Design of collagen-mimetic peptides for heterotrimeric folds

• Self-assembly of collagen mimics for potential biomaterials

• Study of mutation effects on collagen

2. Functionalized peptides for metal sensors and catalysts  

• Based on small peptide motifs, such as β-hairpins, we incorporate specific amino acids in the sequence for the metal sensors with high selectivity and sensitivity

• Using various peptide scaffolds, such as polyproline, α-helices, and β-sheets, to design catalysts

3. Folding study of protein and peptide structures        

• Stereoelectronic effects on polyproline conformation

• The interactions involved in the stabilization of polyproline conformation conversion

• Using proline derivates small peptide models to investiagte how proline puckers affect protein stability

Essentially, our research involves in biochemistry, protein chemistry, physical chemistry, biophysics, and structural biology, and thus the interdisciplinary knowledge and techniques can be learned for further exploring the world beyond chemistry.