Basic Parts
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AAP2 (Acid-activated Peptide)
BBP-M-AAP2
Mechanism of AAP2
AAP2 (Acid-actived Peptide) is one kind of peptides that can kill the Streptococcus. mutans in low pH condition efficiently, which based on the ability of S.mutans to produce acids——leading to the physiological condition leading to caries. AAP2 targeted on the cytoplasmic membrane, as its amino acid composition, amphipathicity, cationic charge and size allow it to attach to and insert into membrane bilayers to form pores by barrel-stave mechanisms. What’s more, inside the AAP2, a alkaline amino carries positive charge in low pH environment can react with a non polar amino to form a more powerful structure that destroy the plasma membrane. So the AAP2 has higher function in low pH but almost non-activated in regular pH.
BBP-M-AAP2
Features of AAP2
T1. pH trigged : The AAP2 is more activated in low pH and this could be its most important feature. The strategy of employing peptides with antimicrobial activity exclusively at low pH could be especially advantageous in dental caries prevention and treatment: cariogenic pathogens would be eliminated due to the local low pH environment surrounding these species, while these peptides should have minimal effect on commensal bacteria that do not produce acid.The resulting shift in microbial dental plaque composition would contribute to neutralizing plaque pH and drive the equilibrium towards tooth surface re-mineralization 2. Small and simple: The coding sequence for a AAP2 is only around 100 base pairs. For E.coli, 100 base pairs is totally within its working capacity. Therefore, E.coli can be a low-cost AAP2 factory, which means more efficient and more product. 3. Secreted directly: Because AAP2 is secreted by the bacterium itself, the bacterium would not form a resistance to it compare to use other inorganic chemicals or antibiotics. Together, using AAP2 is totally a environmental friendly and safe way for solving dental caries in a long term. This part is a coding gene of Targeted Antimicrobial Peptide AAP2&Bac8c. See our AAP2 ( Acid-activated Peptide) parts collection: ######Reference:
Lina Li, Jian He, Randal Eckert, Daniel Yarbrough, Renate Lux, Maxwell Anderson, and Wenyuan Shi. 2010. Design and Characterisation of an Acid-Activated Antimicrobial Peptide. Chem Biol Drug Des. 2010 January ; 75(1): 127–132. Wikipedia; https://en.wikipedia.org/wiki/Antimicrobial_peptides#Mode_of_actionBasic Parts
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Bac8c (Bactenecin）
A coding gene for Bac8c
Mechanism of Bac8c
Bac8c (Bactenecin 8 Peptide) is one kind of peptides that can kill the Streptococcus. mutans in regular pH condition efficiently, which is suitable for average oral environments. Bac8c targeted on the cytoplasmic membrane, as its amino acid composition, amphipathicity, cationic charge and size allow it to attach to and insert into membrane bilayers to form pores by barrel-stave mechanisms.
Features of Bac8c
1. Strong and stable: The Bac8c has less demands about pH condition and it could reach its highest activity, which means it can survive longer in the oral environment with expected activity. 2. Small and simple: The coding sequence for a Bac8c is only around 100 base pairs. For E.coli, 100 base pairs is totally within its working capacity. Therefore, E.coli can be a low-cost Bac8c factory, which means more efficient and more product. 3. Secreted directly: Because Bac8c is secreted by the bacterium itself, the bacterium would not form a resistance to it compare to use other inorganic chemicals or antibiotics. Together, using Bac8c is totally a environmental friendly and safe way for solving dental caries in a long term. This part is a coding gene of Targeted Antimicrobial Peptide AAP2&Bac8c. See our Bac8c ( Bactenecin 8 Peptide) parts collection: #####Reference:
Randal Eckert, Fengxia Qi, Daniel K. Yarbrough, Jian He, Maxwell H. Anderson, and Wenyuan Shi. 2006. Adding Selectivity to Antimicrobial Peptides: Rational Design of a Multidomain Peptide against Pseudomonas spp. Antimicrobial Agents and Chemotherapy, Apr. 2006, p. 1480–148..Basic Parts
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CAP(Competence Stimulating Peptide)
Mechanism of CAP
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