MT-1 Peptide

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MT-1 peptide is a synthetic oligopeptide composed of 11 amino acids (Ac-Ser-Asp-Lys-Pro-Asp-Glu-Ala-Glu-Asp-Ser-OH). Its sequence is derived from the natural substance metallothionein in the human body. It is renowned for its outstanding metal-binding ability (especially for zinc and copper) and powerful antioxidant properties. As a cell protector, it can effectively neutralize free radicals, alleviate oxidative stress, thereby protecting cells from environmental damage and inflammatory attacks, and shows anti-aging potential. It can help maintain cell vitality by supporting telomere maintenance and promoting DNA repair. In the field of skin care, MT-1 peptide is widely used to enhance the natural defense mechanism of the skin, improve elasticity, reduce fine lines and wrinkles, and improve overall skin health and appearance. Additionally, its role in immune regulation and neuroprotection has also attracted much research attention, demonstrating the potential for treating neurodegenerative diseases. Its high biocompatibility and low toxicity make it a safe and multifunctional active ingredient in the fields of biomedicine and cosmetics.

MT-1 Powder COA

MT-1 (Metallothionein-1) is a type of low-molecular-weight protein rich in cysteine. Its core function is to regulate the balance of metal ions in the body through metal chelation, participate in antioxidant defense and detoxify heavy metals. The following elaborates on the metal chelation nature of MT-1 peptides from four dimensions: chemical nature, structural characteristics, functional mechanism and research applications.

Structural Characteristics: The Metal Chelation Foundation of MT-1 Peptide

 

The molecular structure of MT-1 peptide provides a physical basis for its metal chelation function, which is specifically manifested as:

Homocysteine content

MT-1 is composed of approximately 60-68 amino acids, with cysteine accounting for 30% (about 20) of the total, which is much higher than that of ordinary proteins (1%-2%). The sulfhydryl group (-SH) of cysteine is a powerful metal ligand, capable of providing lone pairs of electrons to form coordination bonds with metal ions.

Conserved Cys-X-Cys motif

The cysteines in MT-1 are arranged in the "Cys-X-Cys" (X is any amino acid) pattern, forming two domains: β and γ. This arrangement enables the sulfhydryl groups to be spatially aggregated, facilitating the simultaneous binding of multiple metal ions.

Lack of aromatic amino acids

MT-1 contains almost no aromatic amino acids such as tryptophan and tyrosine, reducing steric hindrance and providing an open coordination environment for metal ions.

Chelation sites and metal capacity:

Zn²⁺/Cd²⁺ binding site: The β domain of MT-1 contains 11 sulfhydryl groups, which can chelate 4 Zn²⁺ or Cd²⁺; the γ domain contains 9 sulfhydryl groups, which can chelate 3 metal ions. A single MT-1 molecule can bind up to 7 divalent metal ions.

Cu⁺ binding site: The binding ability of Cu⁺ to sulfhydryl groups is stronger. MT-1 can chelate up to 12 Cu⁺ to form a more stable complex.

Research applications: Expansion of the metal chelation function of MT-1

01

Biomedical field

Disease markers: The expression level of MT-1 in the peripheral blood of patients with rheumatoid arthritis is positively correlated with disease activity (DAS28), suggesting that it can serve as a biomarker for inflammation and oxidative stress.

Drug carrier: Utilizing the metal chelation property of MT-1, a targeted delivery system can be designed. For example, combining anti-cancer drugs with MT-1, triggering drug release through the high concentration of metal ions in the tumor microenvironment.

02

Environmental science field

Heavy metal pollution remediation: Transgenic plants expressing MT-1 can enhance the absorption and chelation of heavy metals (such as cadmium, lead) for soil remediation.

Biological sensor: Based on the specific binding of MT-1 to metal ions, a highly sensitive heavy metal detection sensor can be developed.

03

Industrial application field

Metal recovery: The strong metal chelation ability of MT-1 can be used to recover precious metals (such as gold, platinum) from industrial wastewater.

Corrosion prevention material: Fixing MT-1 on the surface of materials can extend their lifespan by chelating corrosive metal ions (such as Fe³⁺).

MT-1 peptide is a low molecular weight protein, with its molecular weight typically ranging from 6000 to 7000 daltons. This low molecular weight characteristic enables MT-1 peptide to have a high diffusion rate and bioavailability, allowing it to quickly reach the target site and exert its function. More importantly, the molecular structure of MT-1 peptide is rich in cysteine, with a content of up to 20% to 30%, meaning each MT-1 molecule contains approximately 20 cysteine residues. The sulfhydryl group (-SH) of cysteine is a powerful metal ligand, capable of providing lone pairs of electrons to form coordination bonds with metal ions, thereby endowing MT-1 peptide with strong metal chelating ability. A single MT-1 molecule can bind up to 7 to 12 metal ions, including zinc (Zn²⁺), cadmium (Cd²⁺), copper (Cu⁺), etc., demonstrating its high capacity for metal binding.

The amino acid composition of MT-1 peptide does not contain aromatic amino acids (such as tryptophan, tyrosine, etc.), which reduces steric hindrance and provides an open coordination environment for metal ions. At the same time, cysteine in MT-1 peptide is arranged in a specific pattern, such as "Cys-X-Cys" (X is any amino acid), this arrangement makes the sulfhydryl groups spatially concentrated, facilitating the simultaneous binding of multiple metal ions. In addition, MT-1 peptide also contains a certain amount of amino acids such as glutamic acid and glycine, which further enhance the metal chelating ability of MT-1 peptide by providing coordination atoms such as carboxyl or amino groups.

The molecular structure of the MT-1 peptide is dumbbell-shaped, consisting of two independent domains: the α domain (carboxyl terminus) and the β domain (amino terminus). The α domain contains four metal ion binding sites, capable of binding four divalent metal ions or more than five monovalent metal ions; the β domain contains three metal ion binding sites, capable of binding three divalent metal ions. This domain design enables the MT-1 peptide to simultaneously chelate multiple metal ions, forming a stable metal-protein complex. Moreover, the structure of the MT-1 peptide is highly conserved during biological evolution. The MT-1 peptides of different species have a high similarity in amino acid sequences and spatial structures, ensuring the stability and reliability of its metal chelation function.

The MT-1 peptide forms coordination bonds with metal ions through its sulfhydryl groups, achieving the chelation of metal ions. During the chelation process, the sulfhydryl groups of the MT-1 peptide provide lone pairs of electrons, which form coordination covalent bonds with the empty orbitals of the metal ions, thereby stably binding the metal ions. This chelation effect not only reduces the toxicity of metal ions but also prevents metal ions from participating in redox reactions, reducing the generation of free radicals. For example, the MT-1 peptide can chelate cadmium ions, forming a stable Cd-MT complex, reducing the toxicity of cadmium in the body and promoting its excretion. Similarly, the MT-1 peptide can also chelate copper ions, preventing copper ions from catalyzing the production of harmful substances such as hydroxyl radicals, protecting cells from oxidative damage.

The metal chelation function of the MT-1 peptide holds significant importance in biology. Firstly, it participates in the regulation of metal ion homeostasis in the body, ensuring that the concentration of metal ions within cells remains within an appropriate range, maintaining the activity of enzymes and the normal progression of gene expression. Secondly, the MT-1 peptide exerts detoxification effects by chelating heavy metal ions, protecting cells from the toxic damage caused by heavy metals. Moreover, the MT-1 peptide can inhibit the generation and transmission of free radicals by chelating metal ions, exerting antioxidant defense functions and protecting cells from oxidative stress damage.

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