Technische Universitaet Muenchen

Winfried Meining

Arne Skerra

Evelyn Eggenstein

The present disclosure relates to a collection of novel muteins derived from human &#x3b1;1m (or a1m) polypeptide or a functional homologue thereof. The disclosure further refers to a &#x3b1;1m mutein capable of specifically binding to one or more targets other than a target to which wild-type &#x3b1;1m binds. The disclosure also relates to a method for producing such collection of muteins and a method for isolating a mutein capable of binding one or more such non-natural targets of wild-type &#x3b1;1m polypeptide. These aspects are made possible due to, e.g, the structural elucidation of &#x3b1;1m disclosed herein by the present inventors, an appreciation of ligand-binding sights thereof and, hence, an understanding of which amino acid positions are most suitable for mutagenesis for re-engineering specificity and affinity for any given target while maintaining the secondary and/or tertiary structure of a1m.

Muteins of a1m lipocalin and method of production therefor

The present disclosure relates to a collection of novel muteins derived from human &#x3b1;1m (or a1m) polypeptide or a functional homolog thereof. The disclosure further refers to a &#x3b1;1m mutein capable of specifically binding to one or more targets other than a target to which wild-type &#x3b1;1m binds. The disclosure also relates to a method for producing such collection of muteins and a method for isolating a mutein capable of binding one or more such non-natural targets of wild-type &#x3b1;1m polypeptide. These aspects are made possible due to, e.g, the structural elucidation of &#x3b1;1m disclosed herein by the present inventors, an appreciation of ligand-binding sights thereof and, hence, an understanding of which amino acid positions are most suitable for mutagenesis for re-engineering specificity and affinity for any given target while maintaining the secondary and/or tertiary structure of a1m.

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Zolling, Germany

Winfried Meining