Microelectrode arrays, electrosynthesis, and the optimization of signaling on an inert, stable surface

• Kendra Drayton-White,
• Siyue Liu,
• Yu-Chia Chang,
• Sakashi Uppal and
• Kevin D. Moeller

Beilstein J. Org. Chem. 2022, 18, 1488–1498, doi:10.3762/bjoc.18.156

• interactions [5][6][7]. For example, a binding curve generated for the interaction between an RGD-peptide (C-PEG6-GGRGDGP) and its integrin (α5,β1) target is shown in Figure 4 below. A PEG-linker was added to the RGD-peptide so that the peptide would not be buried in the polymer coating the surface of the

• direct analogy to the RGD-peptide experiment shown above. In this case, a Cu(II)-mediated Chan–Lam coupling reaction was used to place each molecule on a arylborate ester coating the array (Scheme 2) [23]. The Cu(II) needed for the transformation was generated at the selected electrodes by the oxidation

• -peptide/integrin pair. Initially, the amount of RGD-peptide placed on the array was increased to see if we could mimic the experiment with the R6A/ Gαi1 pair that amplified the binding curve out of the observable window. This effort is highlighted in Figure 7. For this experiment, the number of cycles

Peptide stapling by late-stage Suzuki–Miyaura cross-coupling

• Hendrik Gruß,
• Rebecca C. Feiner,
• Ridhiwan Mseya,
• David C. Schröder,
• Michał Jewgiński,
• Kristian M. Müller,
• Rafał Latajka,
• Antoine Marion and
• Norbert Sewald

Beilstein J. Org. Chem. 2022, 18, 1–12, doi:10.3762/bjoc.18.1

• data [72]. Moreover, the epimerization by the conditions of SMC is unlikely as it has been excluded by total hydrolysis of a late-stage SMC modified RGD peptide [67]. Analysis of the secondary structures of the cyclic peptides P2–P4 by CD spectroscopy also did not show a significantly increased α

Synthesis and physicochemical evaluation of fluorinated lipopeptide precursors of ligands for microbubble targeting

• Masayori Hagimori,
• Estefanía E. Mendoza-Ortega and
• Marie Pierre Krafft

Beilstein J. Org. Chem. 2021, 17, 511–518, doi:10.3762/bjoc.17.45

• peptide ligands dramatically increased cellular association in HER2-positive cells. Other lipids grafted to the RGD peptide and SG spacer were integrated in PEGylated liposomes and were efficiently associated with integrin αvβ3-expressing Colon-26 cells [25]. One of our general objectives is to synthesize

Facile synthesis of 7-alkyl-1,2,3,4-tetrahydro-1,8-naphthyridines as arginine mimetics using a Horner–Wadsworth–Emmons-based approach

• Rhys A. Lippa,
• John A. Murphy and
• Tim N. Barrett

Beilstein J. Org. Chem. 2020, 16, 1617–1626, doi:10.3762/bjoc.16.134

• ; Introduction Tetrahydronaphthyridines are prominent in peptidomimetic pharmaceuticals as arginine mimetics and they are widely used in Arg–Gly–Asp (RGD) peptide mimetics such as αv integrin inhibitors [1]. Tetrahydronaphthyridines represent less basic but more permeable alternatives to arginine (pKa ≈ 7 versus

Synthesis and photophysical studies of a multivalent photoreactive Ru^II-calix[4]arene complex bearing RGD-containing cyclopentapeptides

• Sofia Kajouj,
• Lionel Marcelis,
• Alice Mattiuzzi,
• Adrien Grassin,
• Damien Dufour,
• Pierre Van Antwerpen,
• Didier Boturyn,
• Eric Defrancq,
• Mathieu Surin,
• Julien De Winter,
• Pascal Gerbaux,
• Ivan Jabin and
• Cécile Moucheron

Beilstein J. Org. Chem. 2018, 14, 1758–1768, doi:10.3762/bjoc.14.150

• , once incorporated into targeted cancer cells thanks to the multivalent platform. Keywords: anticancer drug; calixarene; cell targeting; RGD peptide; ruthenium complex; Introduction Long-living luminescent polyazaaromatic ruthenium(II) complexes are intensively studied in a biological context, in

On the design principles of peptide–drug conjugates for targeted drug delivery to the malignant tumor site

• Eirinaios I. Vrettos,
• Gábor Mező and
• Andreas G. Tzakos

Beilstein J. Org. Chem. 2018, 14, 930–954, doi:10.3762/bjoc.14.80

• payloads to brain malignancies [78][79]. Cyclic peptide variants have been developed for the RGD peptide motif, reported above. The most commonly used cyclic peptide is iRGD (CRGDKGPDC), a 9-amino acid cyclic peptide, with tumor tissue penetration activity [80]. iRGD initially binds to αVβ3 and αVβ5

Regulation of integrin and growth factor signaling in biomaterials for osteodifferentiation

• Qiang Wei,
• Theresa L. M. Pohl,
• Anja Seckinger,
• Joachim P. Spatz and
• Elisabetta A. Cavalcanti-Adam

Beilstein J. Org. Chem. 2015, 11, 773–783, doi:10.3762/bjoc.11.87

• together for developing new biomaterials to enhance bone regeneration. For example, the microspheres with immobilized RGD peptide and adsorbed BMP-2 exhibits high potential for cell adhesion and differentiation of MSCs [86]. In another case, the pro-osteogenic α2β1 integrin-specific GFOGER peptide ligands

Detonation nanodiamonds biofunctionalization and immobilization to titanium alloy surfaces as first steps towards medical application

• Juliana P. L. Gonçalves,
• Afnan Q. Shaikh,
• Manuela Reitzig,
• Daria A. Kovalenko,
• Jan Michael,
• René Beutner,
• Gianaurelio Cuniberti,
• Dieter Scharnweber and
• Jörg Opitz

Beilstein J. Org. Chem. 2014, 10, 2765–2773, doi:10.3762/bjoc.10.293

• regioselective partial incorporation of biofunctional molecules into anodically grown oxide layers. The authors electrochemically immobilized nucleic acids on titanium alloys for its surface modification with bioactive molecules [21][22][23][24][25], as, e.g., oligonucleotides and RGD peptide conjugates, for

Towards a biocompatible artificial lung: Covalent functionalization of poly(4-methylpent-1-ene) (TPX) with cRGD pentapeptide

• Lena Möller,
• Christian Hess,
• Jiří Paleček,
• Yi Su,
• Axel Haverich,
• Andreas Kirschning and
• Gerald Dräger

Beilstein J. Org. Chem. 2013, 9, 270–277, doi:10.3762/bjoc.9.33

• for Biotechnology and Artificial Organs (LEBAO) Hannover Medical School (MHH), 30625 Hannover, Germany 10.3762/bjoc.9.33 Abstract Covalent multistep coating of poly(methylpentene), the membrane material in lung ventilators, by using a copper-free “click” approach with a modified cyclic RGD peptide

• -norbornadiene 6, by using classical coupling chemistry, which resulted in polymers 7a and 7b, respectively (Scheme 1). The alkyne-containing amino acid 5 was prepared according to Brea et al. [15] Membrane 7a, synthesized from polymer 4 and amino acid 5, was coupled with RGD peptide 1b, bearing an azido group

• grow ECs on TPX membranes. We found that this new TPX membrane 8a showed reduced biological potency to bind ECs. This observation is in accordance with studies by Beer et al. who showed that virtually all RGD binding sites can be reached by integrins, when the distance between the surface and the RGD

Chromo- and fluorophoric water-soluble polymers and silica particles by nucleophilic substitution reaction of poly(vinyl amine)

• Katja Hofmann,
• Ingolf Kahle,
• Frank Simon and
• Stefan Spange

Beilstein J. Org. Chem. 2010, 6, No. 79, doi:10.3762/bjoc.6.79

• with the thiolated RGD peptide cyclo(Arg-Gly_Asp-Phe-Lys(mpa))(c(RGDFK)-SH) leads to a fluorescent sensor for imaging tumor cells [37]. In this paper we report our current studies on the functionalization of PVAm with carbonitrile 1 to introduce a chromophore as well as a fluorophore into the polymer