[1] AL-HALIFA S, BABYCH M, ZOTTIG X, et al. Amyloid self-assembling peptides: potential applications in nanovaccine engineering and biosensing. Peptide Sci. 2019;111(1):2475-8817.
[2] CHEN J, ZOU X. Self-assemble peptide biomaterials and their biomedical applications. Bioact Mater. 2019;4:120-131.
[3] ESKANDARI S, GUERIN T, TOTH I. Recent advances in self-assembled peptides: lmplications for targeted drug delivery and vaccine engineering. Adv Drug Deliv Rev. 2017;110:169-187.
[4] ZHOU J, LI J, DU XW, et al. Supramolecular biofunctional materials. Biomaterials. 2017;129:1-27.
[5] MODLIN I M, KIDD M, FARHADI J. Bayliss and Starling and the nascence of endocrinology. Regul Pept. 2000;93(1):109-123.
[6] SOUTHARD GL, BROOKE GS, PETTEE JM. Solid phase peptide synthesis. I. A mild method of solid phase peptide synthesis employing an enamine nitrogen protecting group and a benzhydryl resin as a solid support. Tetrahedron Lett. 1969;10(40):3505-3508.
[7] BORNSCHEIN W, GOLDMANN FL, DRESSLER J. Diagnostik der exokrinen Pankreasinsuffizienz mit einem synthetischen chymotrypsinspezifischen Peptid. J Mol Med. 1978;56(4):197-205.
[8] RUOSLAHTI E, PIERSCHBACHER M. New perspectives in cell adhesion: RGD and integrins. Science. 1987;238(4826):491-497.
[9] ESTROFF LA, HAMILTON AD. Water gelation by small organic molecules. Chem Rev. 2004;104(3):1201-1217.
[10] STEVENS MM, ALLEN S, SAKATA JK, et al. pH-Dependent behavior of surface-immobilized artificial leucine zipper proteins. Langmuir. 2004;20(18):7747-7752.
[11] WANG H, HEILSHORN SC. Adaptable Hydrogel Networks with Reversible Linkages for Tissue Engineering. Adv Mater. 2015;27(25):3717-3736.
[12] JAYAWARNA V, RICHARDSON S, HIRST A. Introducing chemical functionality in Fmoc-peptide gels for cell culture. Acta Biomater. 2009;5(3):934-943.
[13] DU XQ, LI P, LU SQ, et al. Highly directional co-assembly of 2,6-pyridinedicarboxylic acid and 4-hydroxypyridine based on low molecular weight gelators. J Mol Liq. 2013;180(4):129-134.
[14] DOU XQ, ZHANG D, FENG CL. Wettability of supramolecular nanofibers for controlled cell adhesion and proliferation. Langmuir. 2013;29(49):15359-15366.
[15] LIU GF, JI W, WANG WL, et al. Multiresponsive hydrogel coassembled from phenylalanine and azobenzene derivatives as 3D scaffolds for photoguiding cell adhesion and release. ACS Appl Mater Interfaces. 2015;7(1):301-307.
[16] YAMANAKA M. Development of C3-symmetric Tris-urea low-molecular-weight gelators. Cheminform. 2016;16(2):768-782.
[17] WEIBIN B, LIFANG C. Solvent-induced controllable self-assembly of poly(9,9-dihexylfluorene). Chem Lett. 2014;43(3):331-333.
[18] Lo PY, Lee GY, Zheng JH, et al. Intercalating pyrene with peptide as a novel self-assembly nano-carrier for colon cancer suppression in vitro and in vivo. Mater Sci Eng C. 2020;109:0928-4931.
[19] HANEIN D, GEIGER B, ADDADI L. Differential adhesion of cells to enantiomorphous crystal surfaces. Science. 1994;263(5152):1413-1416.
[20] HARTGERINK JD, BENIASH E, STUPP SI. Self-assembly and mineralization of peptide-amphiphile nanofibers. Science. 2001;294(5547):1684-1688.
[21] LIAO G, WANG L, YU W. Application of novel targeted molecular imaging probes in the earlydiagnosis of upper urinary tract epithelial carcinoma. Oncol Lett. 2018;16(5):6349-6354.
[22] Feng CL, Dou X, Zhang D, et al. A highly efficient self‐assembly of responsive c2‐cyclohexane‐derived gelators. Macromol Rapid Commun. 2012;33(18):1535-1541.
[23] HONG Y, PRITZKER MD, LEGGE RL, et al. Effect of NaCl and peptide concentration on the self-assembly of an ionic-complementary peptide EAK16-II. Colloids Surf B. 2005;46(3):152-161.
[24] KABIRI M, BUSHNAK I, MCDERMOT MT, et al. Toward a mechanistic understanding of ionic self-complementary peptide self-assembly:role of water molecules and ions. Biomacromolecules. 2013;14(11):3943-3950.
[25] MUJEEB A, MILLER AF, SAIANI A, et al. Self-assembled octapeptide scaffolds for in vitro chondrocyte culture. Acta Biomater. 2013;9(1):4609-4617.
[26] KUMAR VA, TAYLOR NL, SHI S, et al. Self-assembling multidomain peptides tailor biological responses through biphasic release. Biomaterials. 2015; 52(1):71-78.
[27] LEI W, PEIPEI Y, XIAOXIAO Z, et al. Self-assembled nanomaterials for photoacoustic imaging. Nanoscale. 2016;8(5):2488-2509.
[28] ZHANG X, CHU X, WANG L, et al. Rational design of a tetrameric protein to enhance interactions between self-assembled fibers gives molecular hydrogels. Angew Chem Int Ed. 2012;51(18):4388-4392.
[29] CARNY O, SHALEV DE, GAZIT E. Fabrication of coaxial metal nanocables using a self-assembled peptide nanotube scaffold. Nano Lett. 2006;6(8):1594-1597.
[30] VAN BOMMEL KJC, VAN DER POL C, MUIZEBELT I, et al. Responsive cyclohexane-based low-molecular-weight hydrogelators with modular architecture. Angew Chem Int Ed. 2004;43(13):1663-1667.
[31] WEISSLEDER R, PITTET MJ. Imaging in the era of molecular oncology. Nature. 2008;452(7187):580-589.
[32] LEE S, XIE J, CHEN X. Peptides and peptide hormones for molecular imaging and disease diagnosis. Chem Rev. 2010;110(5):3087-3111.
[33] FAN Z, SUN L M, HUANG Y J, et al. Bioinspired fluorescent dipeptide nanoparticles for targeted cancer cell imaging and real-time monitoring of drug release. Nat. Nanotechnol. 2016;11(4):388-394.
[34] WU J, ZAWISTOWSKI A, EHRMANN M, et al. Peptide functionalized polydiacetylene liposomes act as a fluorescent turn-on sensor for bacterial lipopolysaccharide. J Am Chem Soc. 2011;133(25):9720-9723.
[35] YANG PP, ZHAO XX, XU AP, et al. Reorganization of self-assembled supramolecular materials controlled by hydrogen bonding and hydrophilic-lipophilic balance. J Mater Chem B. 2016;4(15):2662-2668.
[36] PARK Y, HONG HY, MOON HJ, et al. A new atherosclerotic lesion probe based on hydrophobically modified chitosan nanoparticles functionalized by the atherosclerotic plaque targeted peptides. J Control Release. 2008;128(3):217-223.
[37] He M, Li J, Tan S, et al. Photodegradable Supramolecular Hydrogels with Fluorescence Turn-On Reporter for Photomodulation of Cellular Microenvironments. J Am Chem Soc. 2013;135(50):18718-18721.
[38] TANG Y, WU Z, ZHANG CH, et al. Enzymatic activatable self-assembled peptide nanowire for targeted therapy and fluorescence imaging of tumors. Chem Commun. 2016;52(18):3631-3634.
[39] SUN HY, LIU Y, ZHANG CT, et al. Peptidic β-sheets induce Congo red-derived fluorescence to improve the sensitivity of HIV-1 p24 detection. Anal Methods. 2017;9(7):1185-1189.
[40] WANG L, LI W, LU J, et al. Supramolecular nano-aggregates based on bis(pyrene) derivatives for lysosome-targeted cell imaging. J Phys Chem C. 2013;117(50): 26811-26820.
[41] LIANG G, REN H, RAO J. A biocompatible condensation reaction for controlled assembly of nanostructures in living cells. Nat Chem. 2010;2(1):54-60.
[42] CHIEN MP, THOMPSON MP, BARBACK CV, et al. Enzyme‐Directed Assembly of a Nanoparticle Probe in Tumor Tissue. Adv Mater. 2013;25(26):3599-3604.
[43] WANG D, SU HF, KWOK RTK, et al. Rational design of a water-soluble NIR AIEgen, and its application in ultrafast wash-free cellular imaging and photodynamic cancer cell ablation. Chem Sci. 2018;9(15):3685-3693.
[44] YI H, LEILEI S, YUE S, et al. A fluorescent light-up aggregation-induced emission probe for screening gefitinib-sensitive non-small cell lung carcinoma. Biomater Sci. 2017;5(4):792-799.
[45] DIMA A, BURTON NC, NTZIACHRISTOS V. Multispectral optoacoustic tomography at 64, 128, and 256 channels. J Biomed Opt. 2014;19(3):36021.
[46] MINGHUA X, LV W. Photoacoustic imaging in biomedicine. Rev Sci Instrum. 2006; 77(4):041101.
[47] YANG K, ZHU L, NIE L, et al. Visualization of protease activity in vivo using an activatable photo-acoustic imaging probe based on CuS nanoparticles. Theranostics. 2014;4(2):134-141.
[48] LEVI J, SATHIRACHINDA A, GAMBHIR SS. A high affinity, high stability photoacoustic agent for imaging gastrin releasing peptide receptor in prostate cancer. Clin Cancer Res. 2014;20(14):3721-3729.
[49] ZHANG T, CUI H, FANG CY, et al. Targeted nanodiamonds as phenotype-specific photoacoustic contrast agents for breast cancer. Nanomedicine. 2015;10(4):573-587.
[50] LEVI J, KOTHAPALLI SR, MA TJ, et al. Design, synthesis, and imaging of an activatable photoacoustic probe. J Am Chem Soc. 2010;132(32):11264-11269.
[51] WU X, YU G, LINDNER D, et al. Peptide targeted high-resolution molecular imaging of prostate cancer with MRI. Ame J Nucl Med Mol I. 2014;4(6):525.
[52] ZHANG D, QI GB, ZHAO YX, et al. Photoacoustic imaging: in situ formation of nanofibers from purpurin18-peptide conjugates and the assembly induced retention effect in tumor sites. Adv Mater. 2015;27(40):6125-6130.
[53] DE LA ZERDA A, LIU ZA, BODAPATI S, et al. Ultrahigh sensitivity carbon nanotube agents for photoacoustic molecular imaging in living mice. Nano Lett. 2010;10(6):2168-2172.
[54] WANG Y, HU X, WENG J, et al. A photoacoustic probe for the imaging of tumor apoptosis by caspase‐mediated macrocyclization and self‐assembly. Angew Chem Int Ed. 2019;58(15):4886-4890.
[55] CHEE HL, GAN CRR, NG M, et al. Biocompatible peptide-coated ultrasmall superparamagnetic iron oxide nanoparticles for in vivo contrast-enhanced magnetic resonance imaging. ACS Nano. 2018;12(7):6480-6491.
[56] BULL SR, GULER MO, BRAS RE, et al. Self-assembled peptide amphiphile nanofibers conjugated to MRI contrast agents. Nano Lett. 2005;5(1):1-4.
[57] YE F, JEONG E, JIA Z, et al. A peptide targeted contrast agent specific to fibrin-fibronectin complexes for cancer molecular imaging with MRI. Bioconjug Chem. 2008;19(12):2300-2303.
[58] DIAFERIA C, GIANOLIO E, PALLADINO P, et al. Peptide materials obtained by aggregation of polyphenylalanine conjugates as gadolinium-based magnetic resonance imaging contrast agents. Adv Funct Mater. 2015;25(45):7003-7016.
[59] YE D, SHUHENDLER AJ, PANDIT P, et al. Caspase-responsive smart gadolinium-based contrast agent for magnetic resonance imaging of drug-induced apoptosis. Chem Sci. 2014;5(10):3845-3852.
[60] BECHET D, AUGER F, COULEAUD P, et al. Multifunctional ultrasmall nanoplatforms for vascular-targeted interstitial photodynamic therapy of brain tumors guided by real-time MRI. Nanomedicine. 2015;11(3):657-670.
[61] PRESLAR AT, PARIGI G, MCCLENDON MT, et al. Gd(III) labeled peptide nanofibers for reporting on biomaterial localization in vivo. ACS Nano. 2014;8(7):7325-7332.
[62] WANG T, WANG D, YU H, et al. Intracellularly acid-switchable multifunctional micelles for combinational photo/chemotherapy of the drug-resistant tumor. ACS Nano. 2016;10(3):3496-3508.
[63] DEKRAFFT KE, XIE Z, CAO G, et al. Iodinated nanoscale coordination polymers as potential contrast agents for computed tomography. Angew Chem Int Edit. 2010;48(52):9901-9904.
[64] KHODADUST F, AHMADPOUR S, ALIGHOLIKHAMSEH N, et al. An improved 99mTc-HYNIC-(Ser)3-LTVSPWY peptide with EDDA/tricine as co-ligands for targeting and imaging of HER2 overexpression tumor. Eur J Med Chem. 2018;144:767-773.
[65] RANA S, NISSEN F, MARR A, et al. Optimization of a novel peptide ligand targeting human carbonic anhydrase IX. Plos One. 2012;7(5):1-11.
[66] FLECHSIG P, LINDNER T, LOKTEV A, et al. PET/CT imaging of NSCLC with a αvβ6 integrin-targeting peptide. Mol Imaging Biol. 2019;21(5):973-983.
[67] TORIIHARA A, DUAN H, THOMPSON HM, et al. 18F-FPPRGD2 PET/CT in patients with metastatic renal cell cancer. Eur J Nucl Med Mol I. 2019;46(7):1518-1523.
[68] LI L, WU Y, WANG Z, et al. SPECT/CT imaging of the novel HER2-targeted peptide probe 99mTc-HYNIC-H6F in breast cancer mouse models. J Nucl Med. 2017;58(5):821-826.
[69] ZHENG L, DING X, LIU K, et al. Molecular imaging of fibrosis using a novel collagen-binding peptide labelled with 99mTc on SPECT/CT. Amino Acids. 2017;49(1):89-101.
[70] ZHOU J, DU X, WANG J, et al. Enzyme-instructed self-assembly of peptides containing phosphoserine to form supramolecular hydrogels as potential soft biomaterials. Front Chem Sci Eng. 2017;11(4):509-515.
[71] WU Y, LI L, WANG Z, et al. Imaging and monitoring HER2 expression in breast cancer during trastuzumab therapy with a peptide probe 99mTc-HYNIC-H10F. Eur J Nucl Med Mol I. 2020;47(11):2613-2623.
[72] ZAHID M, FELDMAN KS, GARCIA-BORRERO G, et al. Cardiac targeting peptide, a novel cardiac vector:studies in bio-distribution, imaging application, and mechanism of transduction. Biomolecules. 2018;8(4):147.
[73] KENNEL SJ, STUCKEY A, MCWILLIAMS-KOEPPEN HP, et al. Tc-99m radiolabeled peptide p5 + 14 is an effective probe for spect imaging of systemic amyloidosis. Mol Imaging Biol. 2016;18(4):483-489.
[74] HAYNIE TP. Radionuclide imaging techniques in the detection of cancer. Cancer. 1967;20(5):607-613.
[75] YAN S, FENG W, LELE Z, et al. The experimental study on anti-tumor effect of “1”3”1I-Tyr-octreotide in nude mice bearing human non-small cell lung cancer. Chinese J Nucl Med. 2009;29(1):34-38.
[76] DU S, LUO C, YANG G, et al. Developing PEGylated reversed d-peptide as a novel her2-targeted SPECT imaging probe for breast cancer detection. Bioconjug Chem. 2020;31(8):1971-1980.
[77] JOKAR S, BEHNAMMANESH H, ERFANI M, et al. Synthesis, biological evaluation and preclinical study of a novel 99mTc-peptide: a targeting probe of amyloid-β plaques as a possible diagnostic agent for Alzheimer’s disease. Bioorg Chem. 2020;99:103857.
[78] FAN L, JIARUI Y, SI C, et al. Peptide-rhodamine B probes containing laminin/fibronectin receptor-targeting sequence (YIGSR/RGD) for fluorescent imaging in cancers. Talanta. 2020;212:0039-9140.
[79] HU K, SHANG J, XIE L, et al. PET imaging of VEGFR with a novel 64Cu-labeled peptide. ACS Omega. 2020;5(15):8508-8514.
[80] ZHANG CL, LIU M, WU R, et al. Radiolabeled YSSCREKA peptide for targeting early thrombosis. J Nucl Med. 2018;59:1085.
[81] QIN Y, CHENG S, LI Y, et al. The development of a Glypican-3-specific binding peptide using in vivo and in vitro two-step phage display screening for the PET imaging of hepatocellular carcinoma. Biomater Sci. 2020;8(20):5656-5665.
[82] CHEN F, XIAO Y, SHAO K, et al. PET Imaging of a novel anxal-targeted peptide 18F-Al-NODA-Bn-p-SCN-GGGRDN-IF7 in A431 cancer mouse models. J Labelled Compd Rad. 2020;63(12):494-501.
[83] WANG Q, LI SB, ZHAO YY, et al. Identification of a sodium pump Na+/K+ ATPase α1-targeted peptide for PET imaging of breast cancer. J Control Release. 2018; 281:178-188.
|