2. Adhesive molecules that can stick to proteins or induce their homo- or heterotropic assembly are interesting
Protein engineering
Therapeutic application (Paclitaxel anti cancer drug : microtubule against depolymerisation)
Adhesion to biological systems
Amoeboid motion of white blood cells, which make use of carbohydrate moieties on their surface for the interaction with selectin.
By using electrostatic and hydrogenbonding interactions, the guanidinium ion can form a salt bridge with oxyanions which exists on the surface of the proteins.

4. bovine serum albumin (BSA; 12 μM)
Arg(Gu+)9 (200 μM)
Association constant K (assoc) = 5.8 x 104 M-1
Asn(TEG-Gu+)9 (200 μM)
Association constant, K (assoc) = 2.6 x 105 M-1

5. Association constant, K (assoc) = 3.4 x 105 M-1
Association constant could not be detected by ITC
(a) Asn(TEG-Gu+)9 and (b) G1(Gu+)9OMe (0, 2, 4, 6, 8, and 10 equivalents to BSA)

6. Transmission electron micrographs of microtubules (MTs), prepared with an /tubulin heterodimer (1 mg/mL), GTP (200 μM), and glycerol (10%) in PEM buffer at 37 °C, and then incubated at 15 °C for 20
min with (a), (b) G1(Gu+)9OMe (40 μM), (c) Asn(TEG-Gu+)9 (40 μM), and (d) G0(Gu+)3OMe (120 μM).

7. Homotropic protein assemblies prompted us to investigate if G1(Gu+)9R can also stabilize heterotropic protein conjugates.
The sliding motion of actomyosin is an important biological event, which is induced
by ATP and is responsible for muscle contraction.
ATP is hydrolyzed by myosin ATPase, and a mechanical motion of myosin is generated.
The motion of myosin is translated into the sliding motion of actin filaments
Actomyosin dynamically changes its association constant from approximately 104 to 107M-1 in response to the binding and hydrolysis of ATP.

8. Isothermal titration calorimetry (ITC) profiles in KCl (0.6m)
containing HEPES buffer (20 mm, pH 7.0). a) Titration of myosin (3.5 mm) with G1(Gu+)9OMe (100 mm) in a range of [G1(Gu+)9OMe]/ [myosin] from 0 to 5.2. b) H(ITC) plots calculated from the thermograms of G1(Gu+)9OMe/myosin (K1=8.3x107, K2=4.6x107, K3=1.6x106, and K4=7.1x105M-1).

9. Flow cell setup
The flow cell was covered with a solution of myosin (30 μL, 40 mgmL-1) in HEPES buffer (20 mM, pH 7.0) containing KCl (25 mM) and MgCl2 (5 mM) and incubated for 60 s.
After unbound myosin was rinsed out by injecting myosin-free HEPES buffer (45 μL), the flow cell was filled with a solution of bovine serum albumin (BSA; 0.5 mgmL-1) in HEPES buffer (20 μL) and incubated for 60 s to inactivate the nonfunctionalized parts of the coverslip surface.
Unbound BSA was rinsed out with BSA-free HEPES buffer (45 μL).
The flow cell was filled at 26ºC with an ATPbuffer solution (20 μL) of fluorescently labeled actin filaments (0.8 ng).
Actin filaments (0.8 ng) underwent a sliding motion on the myosin-functionalized coverslip with an average velocity of 4.6 μms-1, which is consistent with the reported value.

10. Heavy meromyosin

11. Summary of papers
developed a new class of molecular glues Asn(TEG-Gu+)9 and G1(Gu+)9R, which bear multiple guanidinium ions as sticky pendants via a flexible oligo(oxyethylene) spacer.
They can adhere to proteins and also stabilize protein assemblies in aqueous buffers due to a multivalent salt-bridge formation between the sticky Gu+ pendants and oxyanionic groups in proteins.
High ability to stabilize microtubules just like that of paclitaxel, suggesting an interesting chemotherapeutic potential of these molecular glues.
They also completely stops the ATP driven sliding motion of Actin over myosin.
By varying the amount of G1(Gu+)9R, the moving velocity of actomyosin can be changed.
Incorporation of stimuli-responsive functionalities into the dendritic molecular glue is one of the interesting subjects that is worthy of further investigation.