Exploiting sequence and stability information for directing nanobody stability engineering.

ABSTRACT:

Background

Variable domains of camelid heavy-chain antibodies, commonly named nanobodies, have high biotechnological potential. In view of their broad range of applications in research, diagnostics and therapy, engineering their stability is of particular interest. One important aspect is the improvement of thermostability, because it can have immediate effects on conformational stability, protease resistance and aggregation propensity of the protein.

Methods

We analyzed the sequences and thermostabilities of 78 purified nanobody binders. From this data, potentially stabilizing amino acid variations were identified and studied experimentally.

Results

Some mutations improved the stability of nanobodies by up to 6.1°C, with an average of 2.3°C across eight modified nano

SUBMITTER: Kunz P 

PROVIDER: S-EPMC5548252 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature