The adsorption of five proteins with very different molecular characteristics, i.e. α-chymotrypsin, human serum albumin, human immunoglobulin, lysozyme, and myoglobin, has been characterized using quantitative fluorescence measurements and atomic force microscopy. It has been found that the 'combinatorial' nature of the micro/nano-channels surface allows for the increased adsorption of molecularly different proteins, comparing with the adsorption on flat surfaces. This amplification increases for proteins with lower molecular surface that can capitalize better on the newly created surface and nano-environments. Importantly, the adsorption on micro/nano-fabricated structures appears to be less dependent on the local molecular descriptors, i.e. hydrophobicity and charges, due to the combinatorialization of the nano-areas presented to the proteins. The amplification of adsorption is important, ranging from 3- to 10-fold, with a higher amplification for smaller, globular proteins.