Types | DnaRegion
|
Roles | Coding
CDS
|
Sequences | BBa_K1647020_sequence (Version 1)
|
Description
The antimicrobial peptide, APP2, can achieve high activity exclusively at low environmental pH to target bacterial species like Streptococcus
mutans that produce acid and thrive under the low pH conditions detrimental for tooth integrity. However, at pH 7.5, it has no effect on cell viability. There are only six histidine(His) and eight phenylalanine(Phe) residues present in the APP2. The pH-responsiveness of APP2 has been attributed to the presence of multiple His which enable the conformational flexibility necessary to transition from the less effective more general membrane disruptive α-helical form at close to neutral pH to its substantially more active random coil conformation at low pH. The hydrophobicity necessary for membrane interaction is provided by Phe groups which in contrast to other hydrophobic amino acids allow for the conformational flexibility needed for the pH-dependent antimicrobial activity of APP2.
Notes
None
Source
None for the moment