Aggregation Resistant Domain Antibodies Selected on Phage by Heat Denaturation  

Oleh:

Jespers, Laurent ; Schon, Oliver ; Famm, Kristoffer ; Winter, Greg

Jenis: Article from Journal - ilmiah internasional
Dalam koleksi: Nature Biotechnology: The Science and Business of Biotechnology vol. 22 no. 9 (Sep. 2004), page 1161-1166.
Topik: HEAT; aggregation resistant; antibodies; heat denaturation

Ketersediaan

Perpustakaan Pusat (Semanggi) Nomor Panggil: NN9.1 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada

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Isi artikel

We describe a method for selecting aggregation resistant proteins by heat denaturation. This is illustrated with antibody heavy chain variable domains (dAbs), which are prone to aggregate. The dAbs were displayed multivalently at the infective tip of filamentous bacteriphage and heated transiently to induce unfolding and to promote aggregation of the dAbs. After cooling, the dAbs weer selected for binding a protein A (A ligand cmmon to these folded dAbs). Phage displaying dAbs that unfold reversibly were thereby enriched with respect to those that do not. From a repertoire of phage dAbs, six dAbs were characterized after selection, they are resisted aggregation, and were soluble, well expressed in bacteria and cold be purified in food yields. The method should be useful for making aggregation resistant proteins and for helping to identify features that promote or prevent protein aggregation, including those responsible for misfolding diseases.

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