An Artificial Design Technique to Optimize Signal Peptide
Gao Cui-Fang, Wang Sen, Tian Feng-Wei, Zhu Ping and Chen Wei
DOI : 10.3844/ajbbsp.2017.114.122
American Journal of Biochemistry and Biotechnology
Volume 13, Issue 3
To determine optimal artificial signal peptide candidates for the possibility of creating high levels of secretion of heterologous proteins, substitution and redesign of amino acid sequences in the H-domain of the signal peptide was theoretically attempted. The method was based on comprehensive score matrix and Markov transfer matrix, which can make the artificial sequences maintain the structural characteristics and original polarity of signal peptides. For the artificial sequence, the feature vector of Structural Fusion Degree (SFD) is first extracted to quantitatively describe the compatibility of artificial cleaved region, then by comparing with highly secreted natural samples; tendencies of specific substitutions in the amino acid sequence can be identified at certain locations. These substitutions may represent the key amino acids that influence the secretion and expression levels of heterologous proteins.
© 2017 Gao Cui-Fang, Wang Sen, Tian Feng-Wei, Zhu Ping and Chen Wei . This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.