Identification of Functional Peptide Sequences to Lead the Design of Precision Polymers

Abstract

Peptide sciences developed dramatically as a result of routine use of solid-phase peptide synthesis and nowadays offer a rich set of well-established strategies to design and identify functional peptide sequences for advanced applications in materials sciences. Appropriate sequences for a wide range of interesting material targets, ranging from molecules to materials surfaces and internal interfaces, can be selected via combinatorial means, and sequence specificities within the resulting peptide-target interactions can be routinely investigated. Based on this understanding, macromolecular sciences can define new polymer structures that meet required functionalities or functional sequences with fully synthetic, nonpeptidic precision polymers to endeavor toward information-based design of next-generation, purpose-adapted macromolecules.

Immobilization of Growth Factors for Cell Therapy Manufacturing

“…For GF immobilization, surfaces are functionalized with specific binding peptides that interact with a pre-loaded GF through different possible modes, such as hydrophobic interactions, recognition of secondary structure motifs, and electrostatic interactions (Stanfield and Wilson, 1995;Wrighton et al, 1996;Fairbrother et al, 1998;Wang et al, 2008). These peptides are often identified by a screening of several sequences that display different properties and thus, bind to their target (in this case GFs) with varying affinity, specificity, and strength (ten Brummelhuis et al, 2017). Specific binding peptides inspired in naturally occurring binding domains may also be used for GF immobilization.…”

PEGylated Precision Segments Based on Sequence‐Defined Thiolactone Oligomers

“…For instance, the sequences in the thiolactone‐based oligomers might be tailored to specifically host drug entities or to adhere to certain material surfaces, leading to precisely adjustable drug solubilizers or surface specific anti‐fouling coatings. Certainly it appears to be an interesting strategy to extract sequence information from peptide based systems, where screening, sequencing, and computational modeling is routine in many laboratories …”

Strategies to Control or Mimic Growth Factor Activity for Bone, Cartilage, and Osteochondral Tissue Engineering

“…GF-binding peptides are commonly identified by screening several sequences that bind to GFs with a range of affinity, specificity, and strength. , For example, phage display has been widely applied to identify peptide sequences that bind strongly and specifically to proteins and other materials. − With a seemingly infinite amount of peptide sequence possibilities, only a select few peptides contain a sequence that binds a specific GF. Peptide sequences can also be derived from naturally occurring binding domains found in ECM biomolecules, such as fibrinogen and fibronectin, which have natural affinities for GFs. ,,, This section will discuss different GF-binding peptide sequences and how they influence GF activity related to bone or cartilage regeneration.…”

“…46,183 GF-binding peptides are commonly identified by screening several sequences that bind to GFs with a range of affinity, specificity, and strength. 46,184 For example, phage display has been widely applied to identify peptide sequences that bind strongly and specifically to proteins and other materials. 184−186 With a seemingly infinite amount of peptide sequence possibilities, only a select few peptides contain a sequence that binds a specific GF.…”