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Propargyl-PEG13-alcohol is a hydrophilic molecule that can react with azide-bearing compounds or biomolecules via copper-catalyzed Click Chemistry to form stable triazole linkages. Its hydrophilic PEG units increase the water-solubility of the molecule, making it suitable for various applications.

1036204-61-1

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1036204-61-1 Usage

Uses

Used in Bioconjugation:
Propargyl-PEG13-alcohol is used as a reactant in the synthesis of fluorescent probes targeting β-amyloid plaques. The hydrophilic PEG units enhance the water-solubility of the molecule, allowing for efficient conjugation with azide-bearing compounds or biomolecules via copper-catalyzed Click Chemistry.
Used in Drug Delivery Systems:
Propargyl-PEG13-alcohol can be used as a component in drug delivery systems, where its hydrophilic nature and ability to form stable triazole linkages can improve the solubility and targeting of therapeutic agents.
Used in Diagnostic Imaging:
The hydrophilic PEG units and stable triazole linkages formed by Propargyl-PEG13-alcohol can be utilized in the development of diagnostic imaging agents, enhancing the contrast and specificity of imaging techniques.
Used in Biosensors:
Propargyl-PEG13-alcohol can be employed in the design of biosensors, where its hydrophilic nature and stable triazole linkages can improve the sensitivity and selectivity of the sensor.
Used in Tissue Engineering:
The hydrophilic PEG units and stable triazole linkages formed by Propargyl-PEG13-alcohol can be utilized in tissue engineering applications, where they can improve the biocompatibility and stability of engineered tissues.

Check Digit Verification of cas no

The CAS Registry Mumber 1036204-61-1 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,0,3,6,2,0 and 4 respectively; the second part has 2 digits, 6 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 1036204-61:
(9*1)+(8*0)+(7*3)+(6*6)+(5*2)+(4*0)+(3*4)+(2*6)+(1*1)=101
101 % 10 = 1
So 1036204-61-1 is a valid CAS Registry Number.

1036204-61-1Downstream Products

1036204-61-1Relevant articles and documents

Design, Synthesis, and Self-Assembly Studies of a Suite of Monodisperse, Facially Amphiphilic, Protein–Dendron Conjugates

Sandanaraj, Britto S.,Bhandari, Pavankumar Janardhan,Reddy, Mullapudi Mohan,Lohote, Akshay Bhagwan,Sahoo, Bankanidhi

, p. 408 - 416 (2020)

The custom design of protein–dendron amphiphilic macromolecules is at the forefront of macromolecular engineering. Macromolecules with this architecture are very interesting because of their ability to self-assemble into various biomimetic nanoscopic structures. However, to date, there are no reports on this concept due to technical challenges associated with the chemical synthesis. Towards that end, herein, a new chemical methodology for the modular synthesis of a suite of monodisperse, facially amphiphilic, protein–dendron bioconjugates is reported. Benzyl ether dendrons of different generations (G1–G4) are coupled to monodisperse cetyl ethylene glycol to form macromolecular amphiphilic activity-based probes (AABPs) with a single protein reactive functionality. Micelle-assisted protein labeling technology is utilized for site-specific conjugation of macromolecular AABPs to globular proteins to make monodisperse, facially amphiphilic, protein–dendron bioconjugates. These biohybrid conjugates have the ability to self-assemble into supramolecular protein nanoassemblies. Self-assembly is primarily mediated by strong hydrophobic interactions of the benzyl ether dendron domain. The size, surface charge, and oligomeric state of protein nanoassemblies could be systematically tuned by choosing an appropriate dendron or protein of interest. This chemical method discloses a new way to custom-make monodisperse, facially amphiphilic, protein–dendron bioconjugates.

Rational Design of Supramolecular Dynamic Protein Assemblies by Using a Micelle-Assisted Activity-Based Protein-Labeling Technology

Sandanaraj, Britto S.,Reddy, Mullapudi Mohan,Bhandari, Pavankumar Janardhan,Kumar, Sugam,Aswal, Vinod K.

, p. 16085 - 16096 (2018/10/15)

The self-assembly of proteins into higher-order superstructures is ubiquitous in biological systems. Genetic methods comprising both computational and rational design strategies are emerging as powerful methods for the design of synthetic protein complexes with high accuracy and fidelity. Although useful, most of the reported protein complexes lack a dynamic behavior, which may limit their potential applications. On the contrary, protein engineering by using chemical strategies offers excellent possibilities for the design of protein complexes with stimuli-responsive functions and adaptive behavior. However, designs based on chemical strategies are not accurate and therefore, yield polydisperse samples that are difficult to characterize. Here, we describe simple design principles for the construction of protein complexes through a supramolecular chemical strategy. A micelle-assisted activity-based protein-labeling technology has been developed to synthesize libraries of facially amphiphilic synthetic proteins, which self-assemble to form protein complexes through hydrophobic interaction. The proposed methodology is amenable for the synthesis of protein complex libraries with molecular weights and dimensions comparable to naturally occurring protein cages. The designed protein complexes display a rich structural diversity, oligomeric states, sizes, and surface charges that can be engineered through the macromolecular design. The broad utility of this method is demonstrated by the design of most sophisticated stimuli-responsive systems that can be programmed to assemble/disassemble in a reversible/irreversible fashion by using the pH or light as trigger.

HYDROPHOBIN MIMICS: PROCESS FOR PREPARATION THEREOF

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Paragraph 0139; 0140; 0390; 0391; 0392-0397; 0493-0500, (2017/09/02)

The present invention discloses hydrophobin mimics of formula (I) comprising a protein head group, hydrophilic linker and hydrophobic tail and to a process for synthesis of library of hydrophobin mimics thereof. The hydrophobin mimics of the present invention self-assemble to form protein nanoparticles/nanocontainer either alone or in a specified chemical environment. The hydrophobin mimics (I) of the present invention find application in area of bio-nanotechnology.

Synthesis of fluorescent probes based on stilbenes and diphenylacetylenes targeting β-amyloid plaques

Parhi, Ajit K.,Kung, Mei-Ping,Ploessl, Karl,Kung, Hank F.

, p. 3395 - 3399 (2008/09/21)

Three fluorescent probes were synthesized aiming for optical imaging to detect amyloid plaques present in the patients with Alzheimer's disease (AD). These compounds were prepared via Sonogashira coupling of a well-defined fluorophore (4-bora-3a,4a-diaza-

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