Material binding peptides are proving to have great potential in improving material synthesis and advancing device fabrication, however, their specificity and interaction mechanisms with target surfaces remain largely elusive. This study contributes to the developing understanding of fundamental principles through which ZnO binding peptides (ZnO-BPs) interact with and modify ZnO growth/morphology. ZnO-BPs used were the reported phage display (PD) identified sequence (G-12 (GLHVMHKVAPPR) and its derivative, GT-16 (GLHVMHKVAPPR-GGGC)) as well as novel sequences generated from post selection modifications including alanine mutants of G-12 (G-12A6, G-12A11, G-12A12) chosen on the basis of peptide stability calculated in silico. Two approaches were used to study interaction of ZnO-BPs with ZnO. Firstly ZnO growth was monitored in the absence and presence of ZnO-BPs during solution synthesis using two different growth routes; the Zn(NO3)2ï¿½6H2O-HMTA system and the ZnAc2-NH3 system. Secondly, isothermal titration calorimetry (ITC) was used to characterize thermodynamic changes during interaction of ZnO with ZnO-BPs. The outcomes of the ZnO synthesis studies demonstrated that a single ZnO-BP can adopt different sequence and concentration dependent mechanisms to control ZnO growth/morphology. The specific synthesis system used dictated the products which ZnO-BPs could interact with and consequently modify crystal nucleation and growth processes. One of the outcomes of the study is the demonstration of the role of histidine within ZnO-BPs in interaction with ZnO and stabilization of LBZs. Analysis of the thermodynamics of ZnO-BP-ZnO crystal interactions using ITC yielded isotherms comprising both an endothermic and an exothermic event. Measured ?G values were between -6 and -8.5 kcal/mol and high adsorption affinity values indicated the occurrence of favourable ZnO-BP-ZnO interactions. Predictive control of material formation processes by peptides can be achieved through a clear understanding of the growth processes and interaction mechanisms.