Sequencing of a fragment of gene encoding pIII minor coat protein showed the presence of 12amino-acids peptide at the N-terminus in almost all phages. Simultaneous analysis of sequenced variants (Table .) shows some conservative motifs in all four independent phage pools recovered after 3 rounds of bio-panning. The peptides DHAQRYGAGHSG (frequency 4 out of 16 proper sequences) and QMGFMTSPKHSV (frequency 8/16 proper sequences) are the most abundant. The isoelectric point (calculated using the online tool PepCalc.com ) of almost all sequenced peptides is above pH 7.4. The recognition steps were performed in PBS, making these peptides positively charged. This result may suggest that these peptides interact with TnT via electrostatic interactions because, in these conditions, the N-terminal region of TnT is negatively charged. In these peptides, predominantly hydrophilic amino acids with hydrogen bond donor groups are present, enabling them to interact with the glutamate-rich regions (which may act as hydrogen bond acceptors). Interaction with the negatively-charged helical Nterminus may play a crucial role in recognising the cardiac TnT isoform due to the tissuespecificity of this region . In conserved central and C-terminal TnT regions, there is a low number of aromatic amino acids (Phe: 6, His: 4, Trp: 3, Tyr: 4); however, this fact and the coincidence with the conservation of His residue in most of the peptides may suggest possible sites of interaction via pi-pi stacking. Additional studies are needed to prove the site where selected peptides may interact with TnT; however, the mentioned conserved positively charged peptides and His residue give hope that the site is located in the cardiac-specific N-terminal region.