Chemical Synthesis of Enamelin Peptide For Tooth Enamel Mimetics and Repair
Disciplines
Biochemistry | Medicinal-Pharmaceutical Chemistry
Abstract (300 words maximum)
Enamelin is one of the crucial matrix proteins associated to the enamel development in teeth and primarily facilitates to grow the enamel surface. In oral health, the teeth are accessory organs that fulfill the roles of digestion and frame the face. The enamel is the hardest substance in the body, composed of proteins as it protects teeth from damage. Over time the enamel can wear down or lose its rigidity, causing discomfort in the mouth. By utilizing solid phase peptide synthesis, we aim to synthesize two important domains of enamelin proteins including Enapep 1, EMFEQDFEKPKEEDPPKAE (218-230) and Enapep-2, EISPPFKEDPGRQEEHLPHPS (571-591). The goal of this project is to understand how these domains strongly bind to the mineral such as calcium ion and involve in the mineralization and promote extreme crystal growth. In long-term, this research also aims to develop peptide-based aprismatic enamel for repair. Enapep-1 and Enapep-2 peptides were synthesized using the solid phase synthesis protocol. In this protocol, high swelling rink amide resin with a loading capacity of .6 mmol/g and 100-200 mesh size was used. After the peptide synthesis, the peptide-resin complexes were cleaved with 95% TFA, 2.5% H2O, and 2.5% Triisopropylsilane. The cleaved peptides were filtered and precipitated by adding cold ether. Then, the precipitate dissolved with 10% acetic acid and lyophilized overnight to form peptide powders. These peptides were characterized by liquid chromatography interfaced with mass spectrometry. The retention time of the Enapep-1 was 2.98 mins which indicated that this peptide is highly soluble and interacted less with the stational phase of the C8 column. Three intense peaks were detected at m/z 581.67, 775.17, and 1162.08 which correspond to [M+4H]4+, [M+3H]3+, and [M+2H]2+ change states, respectively. These experimental masses are exactly agreed with the theoretical masses.
Academic department under which the project should be listed
CSM - Chemistry and Biochemistry
Primary Investigator (PI) Name
Mohammad A. Halim
Chemical Synthesis of Enamelin Peptide For Tooth Enamel Mimetics and Repair
Enamelin is one of the crucial matrix proteins associated to the enamel development in teeth and primarily facilitates to grow the enamel surface. In oral health, the teeth are accessory organs that fulfill the roles of digestion and frame the face. The enamel is the hardest substance in the body, composed of proteins as it protects teeth from damage. Over time the enamel can wear down or lose its rigidity, causing discomfort in the mouth. By utilizing solid phase peptide synthesis, we aim to synthesize two important domains of enamelin proteins including Enapep 1, EMFEQDFEKPKEEDPPKAE (218-230) and Enapep-2, EISPPFKEDPGRQEEHLPHPS (571-591). The goal of this project is to understand how these domains strongly bind to the mineral such as calcium ion and involve in the mineralization and promote extreme crystal growth. In long-term, this research also aims to develop peptide-based aprismatic enamel for repair. Enapep-1 and Enapep-2 peptides were synthesized using the solid phase synthesis protocol. In this protocol, high swelling rink amide resin with a loading capacity of .6 mmol/g and 100-200 mesh size was used. After the peptide synthesis, the peptide-resin complexes were cleaved with 95% TFA, 2.5% H2O, and 2.5% Triisopropylsilane. The cleaved peptides were filtered and precipitated by adding cold ether. Then, the precipitate dissolved with 10% acetic acid and lyophilized overnight to form peptide powders. These peptides were characterized by liquid chromatography interfaced with mass spectrometry. The retention time of the Enapep-1 was 2.98 mins which indicated that this peptide is highly soluble and interacted less with the stational phase of the C8 column. Three intense peaks were detected at m/z 581.67, 775.17, and 1162.08 which correspond to [M+4H]4+, [M+3H]3+, and [M+2H]2+ change states, respectively. These experimental masses are exactly agreed with the theoretical masses.