Phillip Messersmith1,Peyman Delparastan1,Katerina Malollari1,Arianna Avellan1,Kelsey DeFrates1,Joakim Engstrom1,Brylee Tiu1,Kyueui Lee1,Cody Higginson1,Jing Cheng1,Yiran Li1,Yi Cao2
University of California, Berkeley1,Nanjing University2
Phillip Messersmith1,Peyman Delparastan1,Katerina Malollari1,Arianna Avellan1,Kelsey DeFrates1,Joakim Engstrom1,Brylee Tiu1,Kyueui Lee1,Cody Higginson1,Jing Cheng1,Yiran Li1,Yi Cao2
University of California, Berkeley1,Nanjing University2
In mussels, the adhesive proteins that are instrumental for attachment to wet surfaces are known to contain high levels of 3,4-dihydroxy-L-alanine (DOPA), often located adjacent to amino residues such as lysine (Lys). The special synergistic relationship between catechols and amines is a subject of high interest, not only for understanding native proteins but also for informing the design of bioinspired polymers for various applications. In this talk we will describe the interfacial phenomena of mussel-inspired peptides and synthetic polymers, with an emphasis on systems containing catechol and amine functional groups that act synergistically to enhance adhesion at interfaces. Characterization techniques such as single molecule force spectroscopy, colloidal probe spectroscopy and lap shear reveal structure-property relationships across length scales. The results provide new insights into interfacial behavior of native mussel adhesive proteins, and inform the design of novel polymer adhesives, for example pressure sensitive adhesives, high-strength thermoset adhesives, and tissue adhesives.