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The surface accessibility of {\alpha}-bungarotoxin has been investigated byusing Gd2L7, a newly designed paramagnetic NMR probe. Signal attenuationsinduced by Gd2L7 on {\alpha}-bungarotoxin C{\alpha}H peaks of 1H-13C HSQCspectra have been analyzed and compared with the ones previously obtained inthe presence of GdDTPA-BMA. In spite of the different molecular size and shape,for the two probes a common pathway of approach to the {\alpha}-bungarotoxinsurface can be observed with an equally enhanced access of both GdDTPA-BMA andGd2L7 towards the protein surface side where the binding site is located.Molecular dynamics simulations suggest that protein backbone flexibility andsurface hydration contribute to the observed preferential approach of bothgadolinium complexes specifically to the part of the {\alpha}-bungarotoxinsurface which is involved in the interaction with its physiological target, thenicotinic acetylcholine receptor.

The surface accessibility of {\alpha}-bungarotoxin monitored by a novel paramagnetic probe