2020/8/23
Our latest research shows that recombinant GHK peptide has high-efficiency copper ion heavy metal chelation and cardio protection
In recent years, due to the increasing pollution of heavy metals in the environment, even the slow accumulation of low-dose heavy metals will pose a major threat and impact on human health. GHK (Glycyl-Histidyl-Lysine) tripeptide is a short peptide that naturally exists in the human body and is often used in cosmetic products to protect the skin and slow down the aging process. Due to the high price of the blue copper peptide on the market, the research team comprising Professor Kelvin Huang-Chou Chen from National Pingtung University and Professor Chung-Der Hsiao from Chung Yuan Christian University attempted to use gene recombination, expression and purification technology to transfer GHK tripeptide gene into expression plastids with His-Tag and GST-Tag double tags at the N-terminus and TEV restriction site; Substituting E. coli fermentation preparation method for peptide synthesis method, GHK blue copper peptide with high economic value was successfully produced. Subsequently, high-pressure liquid chromatography was used to complete the highly purified GHK peptide. The research team then used UV-visible absorption spectroscopy and near-edge X-ray absorption spectroscopy to study the physical and chemical properties of the recombinant GHK blue copper peptide. Experimental evidence shows that each unit of GHK peptide can form a high-affinity GHK-Cu complex with divalent copper ions in a ratio of 1:1. The research team subsequently used zebrafish as a living experimental model to prove that the recombinant GHK blue copper peptide has the ability to detoxify copper heavy metals and can effectively reverse cardiotoxicity and arrhythmia caused by copper ion exposure. This research has recently been published in "Biomolecules", an high-impact journal in the field of chemical biology. Professor Kelvin Huang-Chou from Department of Applied Chemistry, National Pingtung University, who is the host of the inter-university and cross-field integration team, said that the importance of this research is to provide a method to effectively reduce the production cost of GHK blue copper peptides and provide direct and strong supporting evidence for the biological activity of GHK blue copper peptides that can effectively neutralize the cardiotoxicity of heavy metals. In the meantime, due to the technology of the present invention has high market applicability, a number of biotechnology manufacturers have proceeded to contact the team for technology licensing negotiations.
Reference
Chung-Der Hsiao, Hsin-Hui Wu, Nemi Malhotra, Yen-Ching Liu, Ying-Hsuan Wu, Yu‐Nung Lin, Ferry Saputra, Fiorency Santoso and Kelvin H.-C. Chen*. Expression and Purification of Recombinant GHK Tripeptides to Protect Acute Cardiotoxicity Raised by Waterborne Copper Exposure in Zebrafish. (2020) Biomolecules, 10, 1202, 1-17. doi:10.3390/biom10091202 (SCI; Impact Factor: 4.082, Corresponding author).
2017/8/14
The bacteriohemerythrin from Methylococcus capsulatus (Bath): Crystal structures reveal that Leu114 regulates a water tunnel
The bacteriohemerythrin(McHr) fromMethylococcus capsulatus (Bath) is an oxygen carrier that serves as a transporter to deliver O2 from the cytosol of the bacterial cell body to the particulate methanemonooxygenase residing in the intracytoplasmic membranes for methane oxidation. Herewe report X-ray protein crystal structures of the recombinantwild type (WT)McHr and its L114A, L114Y and L114Fmutants. The structure of the WT reveals a possiblewater tunnel in theMcHr thatmight be linked to its faster autoxidation relative to hemerythrin in marine invertebrates. With Leu114 positioned at the end of this putativewater tunnel, the hydrophobic side chain of this residue seems to play a prominent role in controlling the access of the water molecule required for autoxidation. This hypothesis is examined by comparing the autoxidation rates of the WT McHr with those of the L114A, L114Y and L114F mutants. The biochemical data are correlated with structural insights derived from the analysis of the putative water tunnels in the various McHr proteins provided by the X-ray structures.
Reference: Kelvin H.-C. Chen*, Phimonphan Chuankhayan, Hsin-Hui Wu, Chun-Jung Chen*, Mitsuhiro Fukuda, Steve S.-F. Yu, Sunney I. Chan. The bacteriohemerythrin from Methylococcus capsulatus (Bath): Crystal structures reveal that Leu114 regulates a water tunnel. (2015) J. Inorg. Biochem., 150, 81-89. (SCI; Impact Factor: 3.444; JCR Category Rank 7/44 (Q1) in Chemistry, Inorganic & Nuclear, Co-corresponding and co-first author)
The bacteriohemerythrin from Methylococcus capsulatus (Bath): Crystal structures reveal that Leu114 regulates a water tunnel
The bacteriohemerythrin(McHr) fromMethylococcus capsulatus (Bath) is an oxygen carrier that serves as a transporter to deliver O2 from the cytosol of the bacterial cell body to the particulate methanemonooxygenase residing in the intracytoplasmic membranes for methane oxidation. Herewe report X-ray protein crystal structures of the recombinantwild type (WT)McHr and its L114A, L114Y and L114Fmutants. The structure of the WT reveals a possiblewater tunnel in theMcHr thatmight be linked to its faster autoxidation relative to hemerythrin in marine invertebrates. With Leu114 positioned at the end of this putativewater tunnel, the hydrophobic side chain of this residue seems to play a prominent role in controlling the access of the water molecule required for autoxidation. This hypothesis is examined by comparing the autoxidation rates of the WT McHr with those of the L114A, L114Y and L114F mutants. The biochemical data are correlated with structural insights derived from the analysis of the putative water tunnels in the various McHr proteins provided by the X-ray structures.
Reference: Kelvin H.-C. Chen*, Phimonphan Chuankhayan, Hsin-Hui Wu, Chun-Jung Chen*, Mitsuhiro Fukuda, Steve S.-F. Yu, Sunney I. Chan. The bacteriohemerythrin from Methylococcus capsulatus (Bath): Crystal structures reveal that Leu114 regulates a water tunnel. (2015) J. Inorg. Biochem., 150, 81-89. (SCI; Impact Factor: 3.444; JCR Category Rank 7/44 (Q1) in Chemistry, Inorganic & Nuclear, Co-corresponding and co-first author)