Collagen type I, which is the main component of the skin is found to have several biological roles in addition to structural role. Collagen is now well known to function by interaction with specific cell receptors like integrins and promote cell adhesion and proliferation. Hence use of collagen peptides and hydrolysates in therapeutics has increased tremendously. The aim of the present study was to determine the cell adhesion and proliferative property of short amino acid sequences in type I collagen. In earlier study, a larger peptide was isolated from bovine Achilles tendon collagen which showed cell adhesion in HeLa (epithelial) cell. Probable integrin binding sequences were identified from the larger peptide using bioinformatics tool. The activity of the identified small sequence was confirmed in HeLa cell line. The peptides were coated onto sterile cell culture microtiter plates at different concentrations and incubated for 6h for adhesion and 48h for proliferation assay. Bovine tendon collagen coated dishes were used as positive control. The cell count increased with increasing concentration of peptide when compared with uncoated surface. MTT assay also showed similar results. Proliferation assay was recorded as images, which showed effective proliferation of the cells in peptide coated surface when compared to uncoated surface. Fluorescent staining of the cell nucleus with Hoechst 53328 exhibited no visible DNA fragmentation and active dividing cells were also observed. The cell adhesion and proliferation assay was performed with fibroblast (3T3-L1 cells), keratinocytes (HaCaT) and compared with epithelial (HeLa) cell line. The concentration of peptides with highest cell adhesive and proliferative activity was determined. This basic study on bioactive collagen peptides would provide information for development of biocompatible biomaterials and scaffolds.