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Effect of the Peptide Secondary Structure on the Peptide ARTICLE pubs.acs.org/Langmuir Effect of the Peptide Secondary Structure on the Peptide Amphiphile Supramolecular Structure and Interactions † ‡ § || ^ z z § Dimitris Missirlis,*, , , , Arkadiusz Chworos, ,# Caroline J. Fu, Htet A. Khant, Daniel V. Krogstad, ,£ and ‡ § || Matthew Tirrell , , ,£ ‡ Department of Chemical Engineering, University of California, Santa Barbara, California 93106, United States § Materials Research Laboratory, University of California, Santa Barbara, California 93106, United States Department) of Bioengineering, University of California, Berkeley, California 94720, United States ^ Department of Physics, University of California, Santa Barbara, California 93106-9530, United States #The Centre of Molecular and Macromolecular Studies, Polish Academy of Sciences in Lodz, Sienkiewicza 112, Lodz 90363, Poland z Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, United States £Department of Materials, University of California, Santa Barbara, California 93106, United States bS Supporting Information ABSTRACT: Bottom-up fabrication of self-assembled nano- materials requires control over forces and interactions between building blocks. We report here on the formation and archi- tecture of supramolecular structures constructed from two different peptide amphiphiles. Inclusion of four alanines be- tween a 16-mer peptide and a 16 carbon long aliphatic tail resulted in a secondary structure shift of the peptide headgroups from R helices to β sheets. A concomitant shift in self-assembled morphology from nanoribbons to coreÀshell worm-like mi- celles was observed by cryogenic transmission electron microscopy (cryo-TEM) and atomic force microscopy (AFM). In the presence of divalent magnesium ions, these a priori formed supramolecular structures interacted in distinct manners, highlighting the importance of peptide amphiphile design in self-assembly. ’ INTRODUCTION One approach to enable innate folding of synthetic peptides Self-assembly is a powerful approach to construct advanced that emulate the folding in the whole protein and simultaneously induce the formation of nanosized, peptide-based materials is to functional materials with control over dimensions on the 2,3 nanoscale.1 Peptide-based building blocks have gained the atten- modify them with a hydrophobic fatty acid tail. The resulting tion of bioengineers because their natural origin provides a chimeric molecules, termed peptide amphiphiles (PAs), self- biocompatible and functional platform for construction of assemble because of hydrophobic interactions and stabilize biomaterials.2 Moreover, advances in peptide synthesis enable secondary-structure motifs on their surface as a result of peptide 4 such technologies for scale up to production levels. The chal- tethering and crowding. Apart from the predominant role of lenge, however, remains to control the self-assembly process hydrophobic interactions of the tails, peptide headgroup inter- fi actions are important for controlling stability and the shape in the accurately at the molecular level to fabricate well-de ned materi- À als, whether these are nanosized colloids for drug delivery, aggregated state.4 6 Solution ionic strength and pH have often macroscopic scaffolds for tissue engineering, or coatings.2 been used as the trigger for self-assembly through screening of Nature serves as inspiration for the fabrication of new materi- charges between neighboring peptides.7,8 The effect of ion type als that rely on self-assembly and exhibit well-defined properties. and valency has also been investigated, revealing the possibility of Structural proteins have evolved as molecular building blocks using it to tune interpeptide forces.9,10 Overall, it has become that come together based on interactions, often mediated by evident that the understanding of peptideÀpeptide interactions small folded peptide segments. These peptides are potential is a key not only in determining how peptides behave at the candidates for the design and fabrication of three-dimensional molecular level but also in controlling the macroscopic proper- structural systems. Moreover, they possess inherent biofunction- ties of the formed materials.4,10,11 ality able to guide or interfere with cell behavior depending upon the application in mind. However, short peptides isolated from Received: March 2, 2011 the protein generally lose their capacity to form active, near- Revised: March 26, 2011 native secondary structures. Published: April 13, 2011 r 2011 American Chemical Society 6163 dx.doi.org/10.1021/la200800e | Langmuir 2011, 27, 6163–6170 Langmuir ARTICLE Figure 1. Chemical structure of PAs used in this study. We recently demonstrated that peptide folding of the short folding stability of the peptide headgroups in micelles (panels B 16-mer peptide p53 À (derived from the MDM2-binding site and D of Figure 2). For C A p53, heating the PA solution above 14 29 16 4 þ of tumor suppressor protein p53) could be manipulated by the 60 °C in the presence of divalent Mg2 resulted in nonreversible selection of appropriate linkers that covalently attached it to a precipitation of the micelles, hence the increase in molar palmitic tail.4 The resulting PAs self-assembled into elongated ellipticity at 215 nm above that temperature. ff micelles that exhibited a di erent type and extent of peptide When bound to MDM2, p5314À29 forms an amphipathic fi R secondary structure. Among the ndings, we observed an inter- helix, exposing a hydrophobic face containing Phe19, Trp23, R β 12 esting shift from a predominantly -helical fold to a -sheet and Leu26 side chains. The peptide in solution is mostly structure, when four alanines were introduced between the unstructured, but following PA assembly, its conformational N terminus of p5314À29 and the palmitic tail. Considering that freedom is reduced and folding is energetically favored. Con- both peptide structure and supramolecular assembly are critical sidering the above, we hypothesized that the peptide has a natural ffi R to developing an e cient delivery system of this inhibitory tendency to form an helix, as is the case for C16p53. Interest- peptide, we examine here in detail the supramolecular structure ingly, inclusion of alanines induces β-sheet formation of the of these two PAs and study how these are influenced by a high peptide headgroups. This result is nontrivial considering that þ concentration of Mg2 ions. Our results reveal striking differ- alanines are frequently found in R-helical segments of proteins ences in self-assembly stemming from the folding of the peptide and, therefore, are considered as R-helix-promoting amino into distinct secondary-structure motifs, which have general acids.13 However, alanine-rich peptides forming β sheets have implications for designing biomaterials as well as for studying also been documented in nature, most notably in silk proteins.14 peptide misfolding diseases. We believe that the positioning of alanines close to the hydrophobic core of the PAs and the tendency to minimize the interfacial area between the core and the aqueous phase induce tight peptide ’ RESULTS AND DISCUSSION packing and favor intermolecular hydrogen bonding. The small side chain of alanine, which is beneficial for the formation of R helices, Self-Assembly of PAs. The chemical structures of the PAs can also be viewed as advantageous for tightly packing β sheets. used in our study consist of an aliphatic palmitic tail and an Indeed, a number of studies have used alanines as spacers in PAs to oligopeptide fragment (Figure 1). The two PAs differ solely by 15À17 promote fiber formation through β-sheet stacking. four alanines interposed between the palmitic tail and the amino The capacity of the peptide headgroup to adopt two different acid sequence LSQETFSDLWKLLPEN from peptide p53 À . 14 29 secondary-structure motifs implies that folding of supramolecu- Hydrophobic forces predominantly drive the self-assembly of lar structures is amenable to control. Several examples exist in the these PAs above the critical association concentration (cac) of R approximately 2 μM;4 the corresponding peptides do not self- literature, where a peptide switches between an -helix and a β-sheet conformation in either a reversible or a nonreversible associate at concentrations up to 0.5 mM. Despite the similarity 5,18 in architecture and amino acid content, the inclusion of four manner. Such transformations also bring in mind protein misfolding scenarios, where a certain protein or peptide segment alanines between p5314À29 and the palmitic tail had a striking aggregates in β-sheet fibrils. These amyloid fibers have been effect on headgroup interactions and peptide folding, as demon- 19 strated using circular dichroism (CD) spectroscopy (Figure 2). implicated with various pathologies. Here, the peptides studied CD spectra in 10 mM PBS, well above the cac of the PAs, adopt a controlled conformation in response to self-assembly. It showed that the peptide adopted a mostly R-helical conforma- is noteworthy that this occurs at particular conditions β fi tion in C16p53 assemblies, whereas it formed sheets in (concentration, pH, temperature, etc.), in which the unmodi ed C A p53 assemblies (panels A and C of Figure 2). In the peptides show limited interactions. We therefore propose that 16 4 þ presence of Mg2 ions, the type of secondary structure was not PAs hold potential not only as building blocks of biomaterials but altered and only a small stabilizing effect in folding was observed, also as
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