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MIMS > Antibodies and Small Molecule Drugs > Flashcards

Antibodies and Small Molecule Drugs Flashcards

1
Q

What are extra hypervariable loops known as? What is the rest of the structure called?

A

Complementarity determining regions, framework

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2
Q

How many CDRs are there on the heavy and light chains?

A

3 on each

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3
Q

Which CDR is the most variable?

A

CDR3 on heavy chain

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4
Q

What are constant domains recognised by?

A

FcR receptors

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5
Q

What is the Fc region?

A

CH2 and CH3 domain

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6
Q

Which receptor does IgG bind to?

A

Fc-gamma-R which prevents it being degraded

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7
Q

Which receptor does IgA bind to?

A

Fc-alpha-R - mucosal layer, gut lining, lactation

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8
Q

Which receptor does IgA/M bind to?

A

Fc-alpha/u-R

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9
Q

Which receptor does IgE bind to?

A

Fc-E-R

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10
Q

What recognises constant domains?

A

Complement receptors

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11
Q

WHat do complement receptors circulate as?

A

Inactive precursors

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12
Q

What does the flu immunity antibody do?

A

Blocks sialic acid binding site on haemaglutinin

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13
Q

What kind of binding is there between flu antibody and haemagglutinin?

A

Induced fit

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14
Q

What does C1q do?

A

Recognises constant domain (binds to IgM or IgG antobodies) > conformational change activates C1r protease > leads to complement cascade and membrane attack complex activation > forms pores in cell membrane and leads to cell death and inflammation

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15
Q

What targets are antibodies restricted to?

A

Surface or soluble

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16
Q

What are polyclonal antibodies used for?

A

Research, cheap and easy to produce

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17
Q

What are monoclonal antibodies for?

A

Clinical use because they are pure

18
Q

What is an epitope?

A

Site for the antibody to bind to

19
Q

How do you get polyclonal antibodies?

A

Inject mouse with antigen, get antibodies from more than one B cell whihc will bind to different epitopes

20
Q

How do you make monoclonal antibodies?

A

Fuse antibody producing cells with a myeloma (B cell cancer) > select so unfused cells die > use binding assay to select highest affinity antibodies

21
Q

What is a mAb? What do they cause?

A

Mouse monoclonal antibody - cause human anti-mouse response (HAMA), Fc region interacts poorly with human Fc receptors so reduced half life

22
Q

What are chimeric antibodies?

A

Use mouse variable regions on a human constant region to fix FcR problems

23
Q

What is a humanised antibody?

A

Use CDR grafting - only need the three variable regions from the mouse and get the rest from a human

24
Q

How do you make human antibodies from transgenic mice?

A

Inactivate mice Ig genes in stem cells, introduce human ones, breed them and some mice will only have human antibodies

25
Q

What is an scFv fused by?

A

SHort protein linker

26
Q

What does a FAB fragment do?

A

Binds to toxic/pathogenic region and blocks function

27
Q

How do you make an scFv library?

A

Use PCR to get a VH and VL genes > put them in a plasmid > create population of bacteriophage > check they bind to antigen

28
Q

How do you make scFv be expressed on the surface?

A

Fuse it with a phage coat protein

29
Q

WHy do we use drugs at the top of cascades?

A

At the bottom you need more due to amplification

30
Q

What binds to EGF receptor?

A

ErbB2

31
Q

What does humira/adalimumab do?

A

Generated by phage display, prevent TNF binding to receptor, for RA and Crohn’s

32
Q

How does humira/adalimumab work?

A

Reduces TNF-alpha activity > less cytokines etc. > less inflammatory infiltrate > less apoptosis and basement mebrane invasion > less inflammation

33
Q

How does herceptin work?

A

Binds to ErbB2 but doesn’t affect dimerisation, causes receptor internalisation and controls cytotoxicity

34
Q

What is between the lobes of a kinase?

A

ATP binding site

35
Q

How does tarceva work?

A

Competes with ATP for binding in EGF receptor kinase, kinase closes over it more than ATP, binds more tightly because froms hydrophobic not just hydrogen

36
Q

What is immunoprecipitation?

A

Using an antibody to catch a protein of interest and any proteins that have associated with it (co-immunoprecipitation)

37
Q

How do you identify proteins following immunoprecipitation?

A

Mass spec

38
Q

What is an epitope tag?

A

Like immunoprecipitation but adding a short AA sequence to the protein you’re looking for so you can use higher affinity antibodies

39
Q

What does an interactome show?

A

Which proteins interact with each other

40
Q

How does the Ras signalling cascade work?

A

Growth factor binds to RTK > cytosolic domain autophosphorylated > Grb2 binds to phosphotyrosine peptide segment via its SH2 domain > also binds to Pro rich segments on Sos via its SH3 domains > Sos is activated and exchanged Ras’s GDP to GTP > Ras binds to Raf > then MAP kinase cascade phosphorylates MEK > MEK phosphorylates MAPK > MAPK migrates to nucleus to phosphorylate Fos and Jun > Ras is inactivated by GTP hydrolysis by GTPase activating proteins > returns to resting state using protein phosphatases

MIMS (8 decks)

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